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415-nt CAT mRNA + H2O
?
-
5'-half portion of the E. coli chloramphenicol acetyltransferase mRNA
-
-
?
Bacillus subtilis pre-tRNATrp + H2O
?
Bacillus subtilis tRNACys + H2O
?
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
Escherichia coli pre-tRNAPhe + H2O
?
GT7H + H2O
?
-
complex of SPH2 with 5' half tRNA
-
-
?
GT7HM10 + H2O
?
-
complex of SPH2 with 5' half tRNA
-
-
?
GT7HM20 + H2O
?
-
complex of SPH2 with 5' half tRNA
-
-
?
GT7HM22 + H2O
?
-
complex of SPH2 with 5' half tRNA
-
-
?
human pre-tRNAArg + H2O
?
mt-pre-tRNAArg + H2O
mt-tRNAArg + 3'-leader of tRNA
-
-
-
-
?
mt-pre-tRNAGlu + H2O
mt-tRNAGlu + 3'-leader of tRNA
-
-
-
-
?
mt-pre-tRNAGly + H2O
mt-tRNAGly + 3'-leader of tRNA
-
-
-
-
?
mt-pre-tRNALeu + H2O
mt-tRNALeu + 3'-leader of tRNA
-
-
-
-
?
mt-pre-tRNALys + H2O
mt-tRNALys + 3'-leader of tRNA
-
-
-
-
?
mt-pre-tRNAVal + H2O
mt-tRNAVal + 3'-leader of tRNA
-
-
-
-
?
pre-tRNA(Arg) + H2O
?
-
-
-
-
?
pre-tRNA(Val) + H2O
?
-
-
-
-
?
pre-tRNA-CAG-trailer + H2O
?
-
5'-, 3'-extended chloroplast pre-tRNAPhe
-
-
?
pre-tRNA-CCA-trailer + H2O
?
pre-tRNA-CCAOH-trailer + H2O
?
pre-tRNA9-AspATC + H2O
?
-
-
-
-
?
pre-tRNAArg + H2O
tRNAArg + 3'-leader of tRNA
-
-
-
-
?
pre-tRNAArg(74CCA76) + H2O
?
-
reaction kinetics for in vitro 3'-processing using engineered enzyme variants, in presence of 10 mM Mg2+ or of 0.2 mM Mn2+
-
-
?
pre-tRNAArg(74GUG76) + H2O
?
-
cleavage of pre-tRNAArg(74GUG76) by engineered variants about 7 to more than 16fold less efficient than that of pre-tRNAArg(74CCA76)
-
-
?
pre-tRNAAsp + H2O
?
-
the enzyme catalyzes endonucleolytic tRNA 3' processing
-
-
?
pre-tRNAGlu-CCAN17 + H2O
?
-
-
-
-
?
pre-tRNAGlu-CCUN17 + H2O
?
-
-
-
-
?
pre-tRNAGlu-CUAN17 + H2O
?
-
-
-
-
?
pre-tRNAGlu-UCAN17 + H2O
?
-
-
-
-
?
pre-tRNAGlu-UUAN17 + H2O
?
-
-
-
-
?
pre-tRNAGlu-UUUN17 + H2O
?
-
-
-
-
?
pre-tRNAGly + H2O
?
-
-
-
-
?
pre-tRNAHis-AUG + H2O
?
-
-
-
?
pre-tRNAHis-CCA + H2O
?
-
-
-
?
pre-tRNALeu + H2O
?
-
the enzyme catalyzes endonucleolytic tRNA 3' processing
-
-
?
pre-tRNALeu(CUN) + H2O
?
-
-
-
-
?
pre-tRNALeu(UUR) + H2O
?
-
-
-
-
?
pre-tRNAPhe + H2O
?
-
the enzyme catalyzes endonucleolytic tRNA 3' processing
-
-
?
pre-tRNASer + H2O
?
-
the enzyme catalyzes endonucleolytic tRNA 3' processing
-
-
?
pre-tRNASer(AGY) + H2O
?
-
-
-
-
?
pre-tRNASer(UCN) + H2O
?
-
wild type
-
-
?
pre-tRNASer(UCN)7443C + H2O
?
-
natural tRNA mutant
-
-
?
pre-tRNASer(UCN)7444U + H2O
?
-
natural tRNA mutant
-
-
?
pre-tRNASer(UCN)7445C + H2O
?
-
natural tRNA mutant
-
-
?
pre-tRNASer(UCN)7445G + H2O
?
-
natural tRNA mutant
-
-
?
pre-tRNASer(UCN)7510G + H2O
?
-
natural tRNA mutant
-
-
?
pre-tRNASer(UCN)7511G + H2O
?
-
natural tRNA mutant
-
-
?
pre-tRNASer(UCN)7512G + H2O
?
-
natural tRNA mutant
-
-
?
pre-tRNAThr + H2O
?
-
-
-
-
?
precursor tRNASer(UGA)-M + H2O
mature tRNASer(UGA)-M
precursor tRNASer(UGA)-M + H2O
mature tRNASer(UGA)-M + ?
-
overexpression of untagged TRZ1, but not FLAG-tagged TRZ1, increases the abundance of mature tRNASer(UGA)-M in strain yYH1
-
-
?
precursor tRNATyr + H2O
tRNA + 3' trailer
pretRNA35-MetCAT + H2O
?
-
-
-
-
?
pTyrI + H2O
?
-
pre-tRNATyr from Oenothera berteriana
-
-
?
R-A1 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-ACA19 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-ACA3 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-ASA1 + H2O
?
-
pre-tRNAArg construct with one base-pair addition after the fifth base-pair of the acceptor stem
-
-
?
R-ASA2 + H2O
?
-
pre-tRNAArg construct with two base-pair additions after the fifth base-pair of the acceptor stem
-
-
?
R-ASA3 + H2O
?
-
pre-tRNAArg construct with three base-pair additions after the fifth base-pair of the acceptor stem
-
-
?
R-ASD1 + H2O
?
-
pre-tRNAArg construct with one base-pair deletion after the third base-pair of the acceptor stem
-
-
?
R-ASD2 + H2O
?
-
pre-tRNAArg construct with two base-pair deletions after the third base-pair of the acceptor stem
-
-
?
R-AT12A + H2O
?
-
pre-tRNAArg construct with one additional base-pair in the acceptor stem and one deleted base-pair in the T stem
-
-
?
R-AT12B + H2O
?
-
pre-tRNAArg construct with one deleted base-pair in the acceptor stem and one additional base-pair in the T stem
-
-
?
R-AT14 + H2O
?
-
pre-tRNAArg construct with one base-pair addition in both acceptor and T stems
-
-
?
R-AT16 + H2O
?
-
pre-tRNAArg construct with two base-pair additions in both acceptor and T stems
-
-
?
R-ATM1 + H2O
?
-
small pre-tRNAArg construct
-
-
?
R-ATM10 + H2O
?
-
small pre-tRNAArg construct
-
-
?
R-ATM11 + H2O
?
-
small pre-tRNAArg construct
-
-
?
R-ATM2 + H2O
?
-
small pre-tRNAArg construct
-
-
?
R-ATM3 + H2O
?
-
small pre-tRNAArg construct
-
-
?
R-ATM4 + H2O
?
-
small pre-tRNAArg construct
-
-
?
R-ATM5 + H2O
?
-
small pre-tRNAArg construct
-
-
?
R-ATM7 + H2O
?
-
small pre-tRNAArg construct
-
-
?
R-ATM8 + H2O
?
-
small pre-tRNAArg construct
-
-
?
R-ATM9 + H2O
?
-
small pre-tRNAArg construct
-
-
?
R-ATW + H2O
?
-
small pre-tRNAArg
-
-
?
R-CCA6 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-CCA8 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-CCG + H2O
?
-
pre-tRNAArg construct
-
-
?
R-CUA + H2O
?
-
pre-tRNAArg construct
-
-
?
R-G10 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-G13 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-G15 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-G19 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-G8 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-GCA + H2O
?
-
pre-tRNAArg construct
-
-
?
R-L0 + H2o
?
-
wild type pre-tRNAArg
-
-
?
R-L3 + H2o
?
-
pre-tRNAArg construct
-
-
?
R-L6 + H2o
?
-
pre-tRNAArg construct
-
-
?
R-TASD2 + H2O
?
-
-
-
-
?
R-TSA1 + H2O
?
-
pre-tRNAArg construct with one base-pair addition in the T stem
-
-
?
R-TSA2 + H2O
?
-
pre-tRNAArg construct with two base-pair additions in the T stem
-
-
?
R-TSD1 + H2O
?
-
pre-tRNAArg construct with one base-pair deletion in the T stem
-
-
?
R-TSD2 + H2O
?
-
pre-tRNAArg construct with two base-pair deletions in the T stem
-
-
?
R-U1 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-UCA + H2O
?
-
pre-tRNAArg construct
-
-
?
R-UUU + H2O
?
-
small pre-tRNAArg construct
-
-
?
S-D-lactoylglutathione + H2O
?
-
is a glyoxalase II substrate, tRNase Z has a broad substrate spectrum, is able to process a substrate belonging to a different subclass of the MBL family
-
-
?
T7-5 + H2O
?
-
complex of SPH2 with shorter RNA
-
-
?
T7M7 + H2O
?
-
complex of SPH2 with RNA heptamer
-
-
?
T7M71 + H2O
?
-
complex of SPH2 with RNA heptamer
-
-
?
Thermoplasma acidophilum pre-tRNAPhe + H2O
?
weak cleavage
-
-
?
Thermotoga maritima pre-tRNAArg(CCA) + H2O
?
Thermotoga maritima pre-tRNAArg(GUG) + H2O
?
Thermotoga maritima pre-tRNAMet(CCA) + H2O
?
Thermotoga maritima pre-tRNAMet(UAG) + H2O
?
thymidine 5'-p-nitrophenyl phosphate + H2O
p-nitrophenol + TMP
-
-
-
-
?
thymidine-5-p-nitrophenyl phosphate + H2O
p-nitrophenol + TMP
-
TpNPP substrate, phosphodiesterase activities of tRNase Z on small chromogenic substrates mentioned, structural features of potential model substrates indicated
-
-
?
tRNAHis48 3'+ C + H2O
?
-
-
-
-
?
tRNAHis48 3'+ CC + H2O
?
-
-
-
-
?
tRNATyr + H2O
?
-
wild type tRNA precursor
-
-
?
trnB-THr + H2O
?
-
pre-tRNATHr with a 47 nucleotide 3' trailing sequence and CCA motif, no cleavage
-
-
?
trnI-Thr + H2O
?
-
pre-tRNAThr with a 83 nucleotide 3' trailing sequence, cleavage at one or two bases downstream the discriminator base
-
-
?
trnI-Thr-CAAATG-trailer + H2O
?
-
-
-
-
?
trnI-Thr-CCAATG-trailer + H2O
?
-
-
-
-
?
trnI-Thr-TAAATG-trailer + H2O
?
-
native trailer sequence
-
-
?
trnI-Thr-TCAATG-trailer + H2O
?
-
-
-
-
?
ubiquitin fusion ribosomal protein L40 mRNA + H2O
?
-
-
-
-
?
ubiquitin fusion ribosomal protein L401 mRNA + H2O
?
-
-
-
-
?
ubiquitin fusion ribosomal protein L402 mRNA + H2O
?
-
-
-
-
?
ubiquitin fusion ribosomal protein L403 mRNA + H2O
?
-
-
-
-
?
additional information
?
-
Bacillus subtilis pre-tRNATrp + H2O
?
cleaved well after C75 relatively
-
-
?
Bacillus subtilis pre-tRNATrp + H2O
?
cleaved well after C75 relatively
-
-
?
Bacillus subtilis tRNACys + H2O
?
efficient cleavage
-
-
?
Bacillus subtilis tRNACys + H2O
?
efficient cleavage
-
-
?
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
-
differentiation of tRNase Z variants by 3'-processing activity and their ability to hydrolyze the phosphodiester bond in the chromogenic phosphodiester bis(p-nitrophenyl)phosphate (bpNPP), smallest known tRNase Z substrate, fourteen variants lost ability to hydrolyze bpNPP, seven variants reveal reduced activity
-
-
?
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
-
differentiation of tRNase Z variants by the substrate bis(p-nitrophenyl)phosphate (bpNPP) described, smallest known tRNase Z substrate
-
-
?
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
-
no hydrolysis of the the chromogenic phosphodiester bis(p-nitrophenyl)phosphate (bpNPP) observed
-
-
?
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
-
bpNPP substrate, phosphodiesterase activities of tRNase Z on small chromogenic substrates mentioned, structural features of potential model substrates indicated
-
-
?
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
-
evidences for sigmoidal saturation kinetics with the small chromogenic phosphodiester substrate reviewed
-
-
?
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
-
displays efficient phosphodiesterase activity against bis(p-nitrophenyl) phosphate, which is unusual among the RNase Z family of enzymes
-
-
?
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
-
phosphodiesterase activity
-
-
?
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
-
-
-
-
?
bis(p-nitrophenyl)phosphate + H2O
p-nitrophenol + p-nitrophenyl phosphate
no hydrolysis of the the chromogenic phosphodiester bis(p-nitrophenyl)phosphate (bpNPP) observed
-
-
?
Escherichia coli pre-tRNAPhe + H2O
?
cleavage is barely detected
-
-
?
Escherichia coli pre-tRNAPhe + H2O
?
cleavage is barely detected
-
-
?
GENV7-Env + H2O
?
-
complex of SPH2 with 5' half tRNAArg
-
-
?
GENV7-Env + H2O
?
-
complex of SPH2 with 5' half tRNAArg
-
-
?
human pre-tRNAArg + H2O
?
efficient cleavage
-
-
?
human pre-tRNAArg + H2O
?
efficient cleavage
-
-
?
human pre-tRNAArg + H2O
?
efficient cleavage
-
-
?
IM0 + H2O
?
-
pre-tRNAIle with CCA 3'-trailer sequence
-
-
?
IM0 + H2O
?
-
pre-tRNAIle with CCA 3'-trailer sequence
-
-
?
IM0 + H2O
?
-
pre-tRNAIle with CCA 3'-trailer sequence
-
-
?
IM1 + H2O
?
-
pre-tRNAIle with CCG 3'-trailer sequence
-
-
?
IM1 + H2O
?
-
pre-tRNAIle with CCG 3'-trailer sequence
-
-
?
IM1 + H2O
?
-
pre-tRNAIle with CCG 3'-trailer sequence
-
-
?
IM2 + H2O
?
-
pre-tRNAIle with CUG 3'-trailer sequence
-
-
?
IM2 + H2O
?
-
pre-tRNAIle with CUG 3'-trailer sequence
-
-
?
IM2 + H2O
?
-
pre-tRNAIle with CUG 3'-trailer sequence
-
-
?
IM3 + H2O
?
-
pre-tRNAIle with UUG 3'-trailer sequence
-
-
?
IM3 + H2O
?
-
pre-tRNAIle with UUG 3'-trailer sequence
-
-
?
IM3 + H2O
?
-
pre-tRNAIle with UUG 3'-trailer sequence
-
-
?
IT1 + H2O
?
-
pre-tRNAIle with CCG and 50 nucleotide 3'-trailer sequence
-
-
?
IT1 + H2O
?
-
pre-tRNAIle with CCG and 50 nucleotide 3'-trailer sequence
-
-
?
IT1 + H2O
?
-
pre-tRNAIle with CCG and 50 nucleotide 3'-trailer sequence
-
-
?
IT2 + H2O
?
-
pre-tRNAIle with CUG and 50 nucleotide 3'-trailer sequence
-
-
?
IT2 + H2O
?
-
pre-tRNAIle with CUG and 50 nucleotide 3'-trailer sequence
-
-
?
IT2 + H2O
?
-
pre-tRNAIle with CUG and 50 nucleotide 3'-trailer sequence
-
-
?
IT3 + H2O
?
-
pre-tRNAIle with UUG and 50 nucleotide 3'-trailer sequence
-
-
?
IT3 + H2O
?
-
pre-tRNAIle with UUG and 50 nucleotide 3'-trailer sequence
-
-
?
IT3 + H2O
?
-
pre-tRNAIle with UUG and 50 nucleotide 3'-trailer sequence
-
-
?
ITO + H2O
?
-
pre-tRNAIle with CCA and 50 nucleotide 3'-trailer sequence
-
-
?
ITO + H2O
?
-
pre-tRNAIle with CCA and 50 nucleotide 3'-trailer sequence
-
-
?
ITO + H2O
?
-
pre-tRNAIle with CCA and 50 nucleotide 3'-trailer sequence
-
-
?
pre-tRNA + H2O
?
-
the glycine/proline-rich ZiPD exosite of tRNase Z takes part in the pre-tRNA binding, it is a flexible arm which protrudes from the main protein body
-
-
?
pre-tRNA + H2O
?
-
the glycine/proline-rich ZiPD exosite of tRNase Z takes part in the pre-tRNA binding, it is a flexible arm which protrudes from the main protein body
-
-
?
pre-tRNA + H2O
?
-
the glycine/proline-rich ZiPD exosite of tRNase Z takes part in the pre-tRNA binding, it is a flexible arm which protrudes from the main protein body
-
-
?
pre-tRNA + H2O
?
-
cleaves intron-containing tRNA precursors and 5'-extended pre-tRNAs
-
-
?
pre-tRNA + H2O
?
-
cleaves pre-tRNAs 3' to the discriminator. Pre-tRNA with 3'-trailers harboring partial CCA motifs (C and CC) are cleaved in vitro by Trz 3' to C and CC, respectively, whereas CCA-containing pre-tRNAs are not cleaved, but are bound to the enzyme
-
-
?
pre-tRNA + H2O
?
-
the TM-type exosite of tRNase Z containing a cluster of 4-5 basic amino acid residues takes part in the pre-tRNA binding, it is a flexible arm which protrudes from the main protein body
-
-
?
pre-tRNA-CCA-trailer + H2O
?
-
3'-extended yeast pre-tRNAPhe
-
-
?
pre-tRNA-CCA-trailer + H2O
?
-
3'-extended yeast pre-tRNAPhe
-
-
?
pre-tRNA-CCAOH-trailer + H2O
?
-
3'-mature chloroplast pre-tRNAPhe
-
-
?
pre-tRNA-CCAOH-trailer + H2O
?
-
3'-mature chloroplast pre-tRNAPhe
-
-
?
pre-tRNA-CCAOH-trailer + H2O
?
-
3'-mature chloroplast pre-tRNAPhe
-
-
?
pre-tRNAAla + H2O
?
-
-
-
?
pre-tRNAAla + H2O
?
-
-
-
?
pre-tRNAarg + H2O
?
the new substrate pre-tRNAArg reveals kinetic parameters with wild type tRNase Z similar to those reported for pre-tRNAHis, enzyme concentration of 25 pM
-
-
?
pre-tRNAarg + H2O
?
-
-
-
-
?
pre-tRNAarg + H2O
?
-
cleavage by full-length tRNase ZL and DELTA30 tRNase ZL with the same efficiency
-
-
?
pre-tRNAarg + H2O
?
-
the enzyme catalyzes endonucleolytic tRNA 3' processing
-
-
?
pre-tRNAarg + H2O
?
-
-
-
-
?
pre-tRNAarg + H2O
?
-
-
-
-
?
pre-tRNACys + H2O
?
-
-
-
?
pre-tRNACys + H2O
?
-
-
-
?
pre-tRNACys + H2O
?
-
-
-
-
?
pre-tRNAGlu + H2O
?
-
-
-
-
?
pre-tRNAGlu + H2O
?
-
-
-
-
?
pre-tRNAHis + H2O
?
-
-
-
?
pre-tRNAHis + H2O
?
the nuclear tRNA is processed to an mature tRNA of 72 nucleotides and a 3' trailer of 32 nucleotides
-
-
?
pre-tRNAHis + H2O
?
-
-
-
-
?
pre-tRNAIle + H2O
?
the mitochondrial tRNA is processed to an mature tRNA of 65 nucleotides and a 3' trailer of 75 nucleotides
-
-
?
pre-tRNAIle + H2O
?
-
-
-
-
?
pre-tRNAIle + H2O
?
-
the enzyme catalyzes endonucleolytic tRNA 3' processing
-
-
?
pre-tRNALys + H2O
?
-
-
-
-
?
pre-tRNALys + H2O
?
-
the enzyme catalyzes endonucleolytic tRNA 3' processing
-
-
?
pre-tRNALys + H2O
?
-
-
-
-
?
pre-tRNALys + H2O
?
-
-
-
-
?
pre-tRNATyr + H2O
?
-
-
-
?
pre-tRNATyr + H2O
?
-
-
-
?
pre-tRNATyr + H2O
?
-
-
-
?
pre-tRNATyr + H2O
?
-
-
-
-
?
pre-tRNATyr + H2O
?
-
the enzyme catalyzes endonucleolytic tRNA 3' processing
-
-
?
pre-tRNAVal + H2O
?
-
-
-
-
?
pre-tRNAVal + H2O
?
-
-
-
-
?
precursor tRNASer(UGA)-M + H2O
mature tRNASer(UGA)-M
-
overexpression of ELAC2 increases the abundance of mature tRNASer(UGA)-M in strain yYH1
-
-
?
precursor tRNASer(UGA)-M + H2O
mature tRNASer(UGA)-M
overexpression of wild-type trz1+ in yYH1 cells can cause an increase in nonsense suppression by tRNASer(UGA)-M1, but overexpression of trz1+ cannot overcome the requirement for Sla1p for maturation of tRNASer(UGA)-M
-
-
?
precursor tRNATyr + H2O
tRNA + 3' trailer
all four recombinant tRNase Z proteins have tRNA 3'-processing activity
-
-
?
precursor tRNATyr + H2O
tRNA + 3' trailer
all four recombinant tRNase Z proteins have tRNA 3'-processing activity. TrZL2 processes the precursor less efficiently, which may be due to the fact that this enzyme is difficult to express and only low amounts of recombinant protein can be obtained
-
-
?
R-C1 + H2O
?
-
-
-
-
?
R-C1 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-CCA19 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-CCA19 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-G1 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-G1 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-G3 + H2O
?
-
pre-tRNAArg construct
-
-
?
R-G3 + H2O
?
-
pre-tRNAArg construct
-
-
?
Rib3 + H2O
?
-
substrate with mature 5'tRNA and 3' unprocessed snoRNA
-
-
?
Rib3 + H2O
?
-
5' mature dicistronic tRNAGly-snoR43.1 precursor RNA
-
-
?
Rib4 + H2O
?
-
substrate with mature 5'tRNA
-
-
?
Rib4 + H2O
?
-
5' and 3' mature dicistronic tRNAGly-snoR43.1 precursor RNA
-
-
?
S5L + H2O
?
-
pre-tRNATyr construct with 5 base pairs in the acceptor stem
-
-
?
S5L + H2O
?
-
pre-tRNATyr construct with 5 base pairs in the acceptor stem
-
-
?
S5L + H2O
?
-
pre-tRNATyr construct with 5 base pairs in the acceptor stem
-
-
?
S6L + H2O
?
-
pre-tRNATyr construct with 6 base pairs in the acceptor stem
-
-
?
S6L + H2O
?
-
pre-tRNATyr construct with 6 base pairs in the acceptor stem
-
-
?
S6L + H2O
?
-
pre-tRNATyr construct with 6 base pairs in the acceptor stem
-
-
?
S7L + H2O
?
-
wild type pre-tRNAIle
-
-
?
S7L + H2O
?
-
wild type pre-tRNAIle
-
-
?
S7L + H2O
?
-
wild type pre-tRNAIle
-
-
?
S8L + H2O
?
-
pre-tRNATyr construct with 8 base pairs in the acceptor stem
-
-
?
S8L + H2O
?
-
pre-tRNATyr construct with 8 base pairs in the acceptor stem
-
-
?
S8L + H2O
?
-
pre-tRNATyr construct with 8 base pairs in the acceptor stem
-
-
?
S9L + H2O
?
-
pre-tRNATyr construct with 9 base pairs in the acceptor stem
-
-
?
S9L + H2O
?
-
pre-tRNATyr construct with 9 base pairs in the acceptor stem
-
-
?
S9L + H2O
?
-
pre-tRNATyr construct with 9 base pairs in the acceptor stem
-
-
?
t-RNAHis48 + H2O
?
-
-
-
-
?
t-RNAHis48 + H2O
?
-
-
-
-
?
t-RNAHis48 3'C + H2O
?
-
-
-
-
?
t-RNAHis48 3'C + H2O
?
-
-
-
-
?
t-RNAHis48 3'CC + H2O
?
-
-
-
-
?
t-RNAHis48 3'CC + H2O
?
-
-
-
-
?
T7M7-T3H + H2O
?
-
complex of SPH2 with 5' half tRNAArg
-
-
?
T7M7-T3H + H2O
?
-
complex of SPH2 with 5' half tRNAArg
-
-
?
T7M7-T7HM1 + H2O
?
-
complex of SPH2 with 5' half tRNAArg
-
-
?
T7M7-T7HM1 + H2O
?
-
complex of SPH2 with 5' half tRNAArg
-
-
?
T7M7-T7HM2 + H2O
?
-
complex of SPH2 with 5' half tRNAArg
-
-
?
T7M7-T7HM2 + H2O
?
-
complex of SPH2 with 5' half tRNAArg
-
-
?
Thermotoga maritima pre-tRNAArg(CCA) + H2O
?
weak cleavage
-
-
?
Thermotoga maritima pre-tRNAArg(CCA) + H2O
?
weak cleavage
-
-
?
Thermotoga maritima pre-tRNAArg(CCA) + H2O
?
cleaved very inefficiently. The cleavage site of pre-tRNAArg(CCA) is identified after C75
-
-
?
Thermotoga maritima pre-tRNAArg(CCA) + H2O
?
cleaved very inefficiently. The cleavage site of pre-tRNAArg(CCA) is identified after C75
-
-
?
Thermotoga maritima pre-tRNAArg(CCA) + H2O
?
cleavage is barely detected
-
-
?
Thermotoga maritima pre-tRNAArg(CCA) + H2O
?
cleavage is barely detected
-
-
?
Thermotoga maritima pre-tRNAArg(GUG) + H2O
?
efficient cleavage
-
-
?
Thermotoga maritima pre-tRNAArg(GUG) + H2O
?
efficient cleavage
-
-
?
Thermotoga maritima pre-tRNAArg(GUG) + H2O
?
weak cleavage
-
-
?
Thermotoga maritima pre-tRNAArg(GUG) + H2O
?
cleaved very inefficiently
-
-
?
Thermotoga maritima pre-tRNAArg(GUG) + H2O
?
cleaved very inefficiently
-
-
?
Thermotoga maritima pre-tRNAMet(CCA) + H2O
?
cleaved albeit very inefficiently. Pre-tRNAMet(CCA) and pre-tRNAMet(UAG) are cleaved after C75 and after the discriminator, respectively
-
-
?
Thermotoga maritima pre-tRNAMet(CCA) + H2O
?
cleaved albeit very inefficiently. Pre-tRNAMet(CCA) and pre-tRNAMet(UAG) are cleaved after C75 and after the discriminator, respectively
-
-
?
Thermotoga maritima pre-tRNAMet(UAG) + H2O
?
cleaved albeit very inefficiently. Pre-tRNAMet(CCA) and pre-tRNAMet(UAG) were cleaved after C75 and after the discriminator, respectively
-
-
?
Thermotoga maritima pre-tRNAMet(UAG) + H2O
?
cleaved albeit very inefficiently. Pre-tRNAMet(CCA) and pre-tRNAMet(UAG) were cleaved after C75 and after the discriminator, respectively
-
-
?
tRNA T3 + H2O
?
-
tRNA variant without the anticodon arm
-
-
?
tRNA T3 + H2O
?
-
without anticodon arm
-
-
?
tRNA T6 + H2O
?
-
tRNA variant without the anticodon arm
-
-
?
tRNA T6 + H2O
?
-
without anticodon and variable arm
-
-
?
tRNA(His48) + H2O
?
-
-
-
-
?
tRNA(His48) + H2O
?
-
-
-
-
?
usRNA1 + H2O
?
-
24 nt unstructured RNA
-
-
?
usRNA1 + H2O
?
-
24 nt unstructured RNA
-
-
?
usRNA1 + H2O
?
-
24 nt unstructured RNA
-
-
?
usRNA1 + H2O
?
-
24 nt unstructured RNA, no cleavage observed
-
-
?
usRNA1 + H2O
?
-
24 nt unstructured RNA
-
-
?
usRNA1 + H2O
?
-
24 nt unstructured RNA
-
-
?
usRNA1 + H2O
?
-
24 nt unstructured RNA
-
-
?
usRNA10 + H2O
?
-
40 nt unstructured RNA
-
-
?
usRNA10 + H2O
?
-
40 nt unstructured RNA
-
-
?
usRNA10 + H2O
?
-
40 nt unstructured RNA
-
-
?
usRNA2 + H2O
?
-
24 nt unstructured RNA
-
-
?
usRNA2 + H2O
?
-
24 nt unstructured RNA
-
-
?
usRNA2 + H2O
?
-
24 nt unstructured RNA
-
-
?
usRNA3 + H2O
?
-
28 nt unstructured RNA
-
-
?
usRNA3 + H2O
?
-
28 nt unstructured RNA
-
-
?
usRNA3 + H2O
?
-
28 nt unstructured RNA
-
-
?
usRNA4 + H2O
?
-
39 nt unstructured RNA
-
-
?
usRNA4 + H2O
?
-
39 nt unstructured RNA
-
-
?
usRNA4 + H2O
?
-
39 nt unstructured RNA
-
-
?
usRNA5 + H2O
?
-
26 nt unstructured RNA
-
-
?
usRNA5 + H2O
?
-
26 nt unstructured RNA
-
-
?
usRNA5 + H2O
?
-
26 nt unstructured RNA
-
-
?
usRNA6 + H2O
?
-
26 nt unstructured RNA
-
-
?
usRNA6 + H2O
?
-
26 nt unstructured RNA
-
-
?
usRNA6 + H2O
?
-
26 nt unstructured RNA
-
-
?
usRNA7 + H2O
?
-
24 nt unstructured RNA
-
-
?
usRNA7 + H2O
?
-
24 nt unstructured RNA
-
-
?
usRNA7 + H2O
?
-
24 nt unstructured RNA
-
-
?
usRNA8 + H2O
?
-
43 nt unstructured RNA
-
-
?
usRNA8 + H2O
?
-
43 nt unstructured RNA
-
-
?
usRNA8 + H2O
?
-
43 nt unstructured RNA
-
-
?
usRNA9 + H2O
?
-
22 nt unstructured RNA
-
-
?
usRNA9 + H2O
?
-
22 nt unstructured RNA
-
-
?
usRNA9 + H2O
?
-
22 nt unstructured RNA
-
-
?
additional information
?
-
-
cannot cleave substrates carrying a 3'-CCA motif
-
-
?
additional information
?
-
-
involvement of tRNase Z in mRNA processing
-
-
?
additional information
?
-
-
RNase BN is active on both double- and single-stranded RNA but duplex RNA is preferred. Displays a profound base specificity, showing no activity on runs of C residues. Digestion by RNase BN leads to 3-mers as the limit products, but the rate slows on molecules shorter than 10 nucleotides in length. RNase BN acts as a distributive exoribonuclease on some substrates, releasing mononucleotides and a ladder of digestion products. RNase BN also cleaves endonucleolytically, releasing 3' fragments as short as 4 nucleotides
-
-
?
additional information
?
-
-
involvement of tRNase Z in pre-5S rRNA cleavage
-
-
?
additional information
?
-
-
overexpression of ELAC2 does not appreciably increase the levels of mature tRNALys(CUU) and tRNAVal(AAC)
-
-
?
additional information
?
-
-
PPM1F and DYNC1H1 mRNAs are genuine targets of tRNase ZL guided by 5'-half-tRNAGlu and the 28S rRNA fragment, respectively
-
-
?
additional information
?
-
-
degraded RNA such as a 5'-half-tRNA and an rRNA fragment function as small guide RNA (sgRNA) guide the enzyme to target RNA
-
-
?
additional information
?
-
overexpression of trz1+ does not appreciably increase the levels of mature tRNALys(CUU) and tRNAVal(AAC)
-
-
?
additional information
?
-
overexpression of trz1+ does not appreciably increase the levels of mature tRNALys(CUU) and tRNAVal(AAC)
-
-
?
additional information
?
-
-
overexpression of trz1+ does not appreciably increase the levels of mature tRNALys(CUU) and tRNAVal(AAC)
-
-
?
additional information
?
-
-
tRNA 3'-processing endoribonuclease, member of the metallo-beta-lactamase superfamily
-
-
?
additional information
?
-
-
can cleave 3' to the CCA motif
-
-
?
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Abetalipoproteinemia
Chorea, psychosis, acanthocytosis, and prolonged survival associated with ELAC2 mutations.
Abscess
Genes Contributing to Porphyromonas gingivalis Fitness in Abscess and Epithelial Cell Colonization Environments.
Acidosis, Lactic
Mutations in ELAC2 associated with hypertrophic cardiomyopathy impair mitochondrial tRNA 3'-end processing.
Carcinogenesis
Mutations in ELAC2 associated with hypertrophic cardiomyopathy impair mitochondrial tRNA 3'-end processing.
Carcinogenesis
The product of the candidate prostate cancer susceptibility gene ELAC2 interacts with the gamma-tubulin complex.
Carcinoma
Association of hereditary prostate cancer gene polymorphic variants with sporadic aggressive prostate carcinoma.
Cardiomyopathies
ELAC2/RNaseZ-linked cardiac hypertrophy in Drosophila melanogaster.
Cardiomyopathies
The Phenotype and Outcome of Infantile Cardiomyopathy Caused by a Homozygous ELAC2 Mutation.
Cardiomyopathy, Dilated
Concerted regulation of mitochondrial and nuclear non-coding RNAs by a dual-targeted RNase Z.
Cardiomyopathy, Hypertrophic
A homozygous splicing mutation in ELAC2 suggests phenotypic variability including intellectual disability with minimal cardiac involvement.
Cardiomyopathy, Hypertrophic
ELAC2 Mutations Cause a Mitochondrial RNA Processing Defect Associated with Hypertrophic Cardiomyopathy.
Cardiomyopathy, Hypertrophic
Mutations in ELAC2 associated with hypertrophic cardiomyopathy impair mitochondrial tRNA 3'-end processing.
Chorea
Chorea, psychosis, acanthocytosis, and prolonged survival associated with ELAC2 mutations.
Infections
ELAC2, an Enzyme for tRNA Maturation, Plays a Role in the Cleavage of a Mature tRNA to Produce a tRNA-Derived RNA Fragment During Respiratory Syncytial Virus Infection.
Infections
Genes Contributing to Porphyromonas gingivalis Fitness in Abscess and Epithelial Cell Colonization Environments.
Infertility, Male
The structural characteristics and the substrate recognition properties of RNase ZS1.
Infertility, Male
The transcription factor GATA10 regulates fertility conversion of a two-line hybrid tms5 mutant rice via the modulation of UbL40 expression.
Intellectual Disability
A homozygous splicing mutation in ELAC2 suggests phenotypic variability including intellectual disability with minimal cardiac involvement.
Mitochondrial Diseases
Mutations in ELAC2 associated with hypertrophic cardiomyopathy impair mitochondrial tRNA 3'-end processing.
Mitochondrial Diseases
Naturally Occurring Mutations in Human Mitochondrial Pre-tRNASer(UCN) Can Affect the Transfer Ribonuclease Z Cleavage Site, Processing Kinetics, and Substrate Secondary Structure.
nadh:ubiquinone reductase (h+-translocating) deficiency
A homozygous splicing mutation in ELAC2 suggests phenotypic variability including intellectual disability with minimal cardiac involvement.
nadh:ubiquinone reductase (h+-translocating) deficiency
ELAC2 Mutations Cause a Mitochondrial RNA Processing Defect Associated with Hypertrophic Cardiomyopathy.
Neoplasm Metastasis
Nuclear ELAC2 overexpression is associated with increased hazard for relapse after radical prostatectomy.
Neoplasms
A novel class of small RNAs: tRNA-derived RNA fragments (tRFs).
Neoplasms
ELAC2 polymorphisms and prostate cancer risk: a meta-analysis based on 18 case-control studies.
Neoplasms
Genetic determinants of prostate cancer: a review.
Neoplasms
Nuclear ELAC2 overexpression is associated with increased hazard for relapse after radical prostatectomy.
Neoplasms
Prostate cancer: simplicity to complexity.
Neoplasms
Single and multivariate associations of MSR1, ELAC2, and RNASEL with prostate cancer in an ethnic diverse cohort of men.
Neoplasms
The product of the candidate prostate cancer susceptibility gene ELAC2 interacts with the gamma-tubulin complex.
Neoplasms
TRUE Gene Silencing: Screening of a Heptamer-type Small Guide RNA Library for Potential Cancer Therapeutic Agents.
Pericardial Effusion
The Phenotype and Outcome of Infantile Cardiomyopathy Caused by a Homozygous ELAC2 Mutation.
Prostatic Diseases
ELAC2 polymorphisms and prostate cancer risk: a meta-analysis based on 18 case-control studies.
Prostatic Neoplasms
A candidate prostate cancer susceptibility gene at chromosome 17p.
Prostatic Neoplasms
A candidate prostate cancer susceptibility gene encodes tRNA 3' processing endoribonuclease.
Prostatic Neoplasms
A novel class of small RNAs: tRNA-derived RNA fragments (tRFs).
Prostatic Neoplasms
A Study of Ser217Leu and Ala541Thr Polymorphism in the Men Afflicted with Prostate Cancer and in the Men being Suspicious of Prostate Cancer.
Prostatic Neoplasms
A survey of green plant tRNA 3'-end processing enzyme tRNase Zs, homologs of the candidate prostate cancer susceptibility protein ELAC2.
Prostatic Neoplasms
Association between RNASEL, MSR1, and ELAC2 single nucleotide polymorphisms and gene expression in prostate cancer risk.
Prostatic Neoplasms
Association of common missense changes in ELAC2 ( HPC2) with prostate cancer in a Japanese case-control series.
Prostatic Neoplasms
Association of hereditary prostate cancer gene polymorphic variants with sporadic aggressive prostate carcinoma.
Prostatic Neoplasms
Characterization of linkage disequilibrium structure, mutation history, and tagging SNPs, and their use in association analyses: ELAC2 and familial early-onset prostate cancer.
Prostatic Neoplasms
Characterization of TRZ1, a yeast homolog of the human candidate prostate cancer susceptibility gene ELAC2 encoding tRNase Z.
Prostatic Neoplasms
ELAC2 and prostate cancer risk in Afro-Caribbeans of Tobago.
Prostatic Neoplasms
ELAC2 polymorphisms and prostate cancer risk: a meta-analysis based on 18 case-control studies.
Prostatic Neoplasms
ELAC2, a putative prostate cancer susceptibility gene product, potentiates TGF-beta/Smad-induced growth arrest of prostate cells.
Prostatic Neoplasms
ELAC2/HPC2 polymorphisms, prostate-specific antigen levels, and prostate cancer.
Prostatic Neoplasms
Genetic analysis of the principal genes related to prostate cancer: A review.
Prostatic Neoplasms
Genetic determinants of prostate cancer: a review.
Prostatic Neoplasms
Genome-wide scan for prostate cancer susceptibility genes using families from the University of Michigan prostate cancer genetics project finds evidence for linkage on chromosome 17 near BRCA1.
Prostatic Neoplasms
Identification and analysis of candidate fungal tRNA 3'-end processing endonucleases tRNase Zs, homologs of the putative prostate cancer susceptibility protein ELAC2.
Prostatic Neoplasms
Integration of copy number and transcriptomics provides risk stratification in prostate cancer: A discovery and validation cohort study.
Prostatic Neoplasms
Meta-analysis of associations of the Ser217Leu and Ala541Thr variants in ELAC2 (HPC2) and prostate cancer.
Prostatic Neoplasms
Molecular biology in prostate cancer.
Prostatic Neoplasms
Mutation screening and association study of RNASEL as a prostate cancer susceptibility gene.
Prostatic Neoplasms
Mutational analysis of susceptibility genes RNASEL/HPC1, ELAC2/HPC2, and MSR1 in sporadic prostate cancer.
Prostatic Neoplasms
Mutations in ELAC2 associated with hypertrophic cardiomyopathy impair mitochondrial tRNA 3'-end processing.
Prostatic Neoplasms
Nuclear ELAC2 overexpression is associated with increased hazard for relapse after radical prostatectomy.
Prostatic Neoplasms
Nucleases of the metallo-beta-lactamase family and their role in DNA and RNA metabolism.
Prostatic Neoplasms
Perspective: prostate cancer susceptibility genes.
Prostatic Neoplasms
Prevalence of the Ser217Leu Variant of the ELAC2 Gene and Its Association with Prostate Cancer in Population of the Littoral Region of Cameroon.
Prostatic Neoplasms
Prevalent mutations in prostate cancer.
Prostatic Neoplasms
Prognostic role of genetic biomarkers in clinical progression of prostate cancer.
Prostatic Neoplasms
Sequence variants of elaC homolog 2 (Escherichia coli) (ELAC2) gene and susceptibility to prostate cancer in the Health Professionals Follow-Up Study.
Prostatic Neoplasms
Single and multivariate associations of MSR1, ELAC2, and RNASEL with prostate cancer in an ethnic diverse cohort of men.
Prostatic Neoplasms
Structure of primate and rodent orthologs of the prostate cancer susceptibility gene ELAC2.
Prostatic Neoplasms
The Caenorhabditis elegans homolog of the putative prostate cancer susceptibility gene ELAC2, hoe-1, plays a role in germline proliferation.
Prostatic Neoplasms
The missense mutations in the candidate prostate cancer gene ELAC2 do not alter enzymatic properties of its product.
Prostatic Neoplasms
The product of the candidate prostate cancer susceptibility gene ELAC2 interacts with the gamma-tubulin complex.
Respiratory Syncytial Virus Infections
ELAC2, an Enzyme for tRNA Maturation, Plays a Role in the Cleavage of a Mature tRNA to Produce a tRNA-Derived RNA Fragment During Respiratory Syncytial Virus Infection.
Severe Combined Immunodeficiency
Nucleases of the metallo-beta-lactamase family and their role in DNA and RNA metabolism.
Starvation
Retrograde nuclear import of tRNA precursors is required for modified base biogenesis in yeast.
Virus Diseases
ELAC2, an Enzyme for tRNA Maturation, Plays a Role in the Cleavage of a Mature tRNA to Produce a tRNA-Derived RNA Fragment During Respiratory Syncytial Virus Infection.
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evolution
Trz1 is organized into two beta-lactamase domains connected by a long linker. The N-terminal domain has lost its catalytic residues, but retains the long flexible arm that is important for tRNA binding, while it is the other way around in the C-terminal domain. Trz1 likely evolved from a duplication and fusion of the gene encoding the monomeric short form RNase Z
additional information
-
Schizosaccharomyces pombe contains two candidate tRNase ZLs encoded by the essential genes sptrz1+ and sptrz2+
malfunction
deletion of the chloroplastic TrZS2 gene results in an embryo-lethal phenotype
malfunction
-
ELAC2 lacking a putative mitochondrial targeting signal (aa 1-30), but not ELAC2 lacking a putative nuclear localization signal (aa 28-35) can increase suppression of ade6-704 in strain yYH1
malfunction
-
in a mutant strain, the chromosomal tRNase Z gene is put under control of an IPTG-dependent promoter. Removal of IPTG from the culture medium results in complete growth inhibition, tRNase Z is essential for the organism. Downregulation of Trz expression leads to an accumulation of CCA-less pre-tRNAs in vivo
malfunction
-
strains with simultanoeus deletion of genes from RNases II, Z, D, T and PH are not viable, but cells survive when only one of these genes is active
malfunction
The knockout TrZL1 mutant shows no visible phenotype
malfunction
The knockout TrZL2 and TrZS1 mutants show no visible phenotypes
malfunction
-
silencing of the gene MRPP1 encoding a subunit of the enzyme leads to inhibition of both 5' and 3' processing
malfunction
-
disruption of TRZ2 is responsible for a mutant albino phenotype with deficient chlorophyll content
malfunction
-
enzyme inactivation compromises nuclear and mitochondrial tRNA 3'-end processing
malfunction
-
RNZED24 knockout mutation causes early larval lethality. RNaseZ knockout completely blocks tRNA maturation without diminishing the abundance of mature tRNA molecules, affects the nuclear-cytoplasmic distribution of tRNA, decreases cell proliferation but not cell survival, and affects maginal disc growth autonomously
malfunction
the specific deletion of ELAC2 in the hearts of mice causes a profound cardiomyopathy and premature death by 4 weeks of age
malfunction
-
enzyme inactivation compromises nuclear and mitochondrial tRNA 3'-end processing
-
metabolism
the enzyme has a major role in the processing of nuclear tRNAs in vivo
metabolism
trz2 overexpression is toxic to cells. It leads to apoptotic cell death. Overexpression of trz2 also caused a loss of mitochondrial membrane potential and an increased reactive oxygen species formation. Overexpressing trz2 increases the level of intracellular iron by about 2fold. trz2 overexpression may cause mitochondrial dysfunction, which is likely to lead to perturbation of iron homeostasis, ROS accumulation and induction of apoptotic cell death in Schizosaccharomyces pombe
metabolism
-
trz2 overexpression is toxic to cells. It leads to apoptotic cell death. Overexpression of trz2 also caused a loss of mitochondrial membrane potential and an increased reactive oxygen species formation. Overexpressing trz2 increases the level of intracellular iron by about 2fold. trz2 overexpression may cause mitochondrial dysfunction, which is likely to lead to perturbation of iron homeostasis, ROS accumulation and induction of apoptotic cell death in Schizosaccharomyces pombe
-
physiological function
Arabidopsis encodes four tRNase Z, two short forms (TrZS1 and TrZS2) and two long forms (TrZL1 and TrZL2)
physiological function
Arabidopsis encodes four tRNase Z, two short forms (TrZS1 and TrZS2) and two long forms (TrZL1 and TrZL2). The mitochondrial tRNase Z protein TrZL2 cleaves tRNA-like elements that serve as processing signals in mitochondrial mRNA maturation
physiological function
Arabidopsis encodes four tRNase Z, two short forms (TrZS1 and TrZS2) and two long forms (TrZL1 and TrZL2). TrZL1 is the only tRNase Z responsible for the maturation of nuclear tRNAs. The mitochondrial tRNase Z proteins TrZL1 cleave tRNA-like elements that serve as processing signals in mitochondrial mRNA maturation
physiological function
-
cytosolic tRNase ZL modulates gene expression through 5'-half-tRNA. The tRNase ZL is likely to be involved in the p53 signaling pathway and apoptosis
physiological function
-
cytosolic tRNase ZL modulates gene expression through a subset of microRNAs in the cells. MiR-103 can form a hook structure to guide target RNA cleavage by cytosolic tRNase ZL in vitro. MiR-103 downregulates gene expression through directing mRNA cleavage by tRNase ZL
physiological function
flexible arm of tRNase Z consists of 3540 residues in a globular, compact alphaalphabetabetaeta structure (the hand) extruded from the body of the enzyme and held apart from it by an extended two-stranded polypeptide stalk
physiological function
-
humans contain one tRNaseZL encoded by the prostate-cancer susceptibility gene ELAC2. Wild-type overproduced from pREP4X, but not from pREP82X, can increase suppression of the UGA nonsense mutation ade6-704 in strain yYH1, through facilitating 3' end processing of the defective suppressor tRNA that mediates suppression. This is dependent on its endonucleolytic activity and its putative nuclear localization signal. Overexpression of ELAC1 cannot increase suppression. ELAC2 can rescue a temperature-sensitive allele of Schizosaccharomyces pombe trz1+, trz1-1, but not the trz1 null mutant
physiological function
-
is not essential for cell viability, role in RNA metabolism. May also work as a backup 3'-maturation enzyme for pre-tRNAs with incorrect nucleotides incorporated into the CCA triplet
physiological function
-
is required for maturation of pre-tRNAs lacking a CCA motif and is thus essential for cell viability
physiological function
-
Saccharomyces cerevisiae contains one tRNase ZL (long form) encoded by the trz1 gene. TRZ1 can complement a temperature-sensitive allele of Schizosaccharomyces pombe trz1+, trz1-1, but not the Schizosaccharomyces pombe trz1 null mutant. Overexpression of TRZ1 can increase suppression of the UGA nonsense mutation ade6-704 through facilitating 3' end processing of the defective suppressor tRNA that mediates suppression
physiological function
Schizosaccharomyces pombe contains two tRNase ZL (long form), encoded by trz1+ and trz2+. Both trz1+ and trz2+ are essential for growth. Ectopic expression of FLAG-tagged trz1+ and trz2+ can fully complement trz1+ and trz2+ disruption, respectively. Overexpression of trz2+ cannot increase suppression
physiological function
Schizosaccharomyces pombe contains two tRNase ZL (long form), encoded by trz1+ and trz2+. Both trz1+ and trz2+ are essential for growth. Trz1+ is required for cell viability in the absence of Sla1p, which is required for endonuclease-mediated maturation of pre-tRNA 3' ends. Overexpression of trz1+ can increase suppression of the UGA nonsense mutation ade6-704 through facilitating 3' end processing of the defective suppressor tRNA that mediates suppression, thus can promote defective tRNA 3' processing in vivo. Both Saccharomyces cerevisiae TRZ1 and human ELAC2 can complement a temperature-sensitive allele of Schizosaccharomyces pombe trz1+, trz1-1, but not the trz1 null mutant. Ectopic expression of FLAG-tagged trz1+ and trz2+ can fully complement trz1+ and trz2+ disruption, respectively. Wild-type cannot increase suppression in the absence of sla1+
physiological function
-
accurate tRNA processing in crucial for mitochondrial genom expression. ELAC2 functions as a mitochondrial tRNase, it cleaves preferentially molecules already processed by mtRNase P
physiological function
-
in addition to tRNase Z, RNase BN of Escherichia coli can act on tRNA precursors containing or lacking a CCA sequence and that it can do so as either an exoribonuclease or an endoribonuclease, overview. Addition of Co2+ results in higher activity and predominantly exoribonucleolytic activity, whereas in the presence of Mg2+ RNase BN is primarily an endoribonuclease. Certain tRNA precursors are extremely poor substrates, overview
physiological function
-
RNase Z is an endonuclease responsible for the removal of 39 extensions from tRNA precursors, an essential step in tRNA biogenesis. Human cells contain a long form RNase ZL, encoded by ELAC2, and a short form RNase ZS, ELAC1. Isozyme RNase ZL is the enzyme involved in both, nuclear and mitochondrial tRNA 39 end maturation
physiological function
-
RNase Z activity is essential for all phases of fly development that involve cell division, including growth of adult tissue progenitors during larval and metamorphic stages, and gametogenesis in adults
physiological function
-
RNase ZS1 controls thermosensitive genic male sterility in rice
physiological function
-
Schizosaccharomyces pombe has two tRNase Z genes, trz1 and trz2, required for nuclear and mitochondrial tRNA 3'-end processing, respectively. In addition, trz2 is also involved in generation of the 5'-ends of other mitochondrial RNAs, whose 5'-ends coincide with the 3'-end of tRNA
physiological function
-
the tRNA 3' processing activity of tRNase Z2 contributes to chloroplast biogenesis
physiological function
-
degraded RNA such as a 5'-half-tRNA and an rRNA fragment function as small guide RNA (sgRNA) guide the enzyme to target RNA
physiological function
endonucleolytically removes 3' trailers from precursor tRNAs, preparing them for CCA addition and aminoacylation
physiological function
the enzyme is involved in nuclear and mitochondrial tRNA 3'-end processing
physiological function
trz1 is responsible for the 3'-end processing of tRNA precursors, which is one of the essential steps in tRNA maturation. Trz1 is involved in nuclear tRNA 3'-end processing
physiological function
trz2 is responsible for the 3'-end processing of tRNA precursors, which is one of the essential steps in tRNA maturation. Trz2 is involved in nuclear tRNA 3'-end processing
physiological function
-
the enzyme is involved in nuclear and mitochondrial tRNA 3'-end processing
-
physiological function
-
trz2 is responsible for the 3'-end processing of tRNA precursors, which is one of the essential steps in tRNA maturation. Trz2 is involved in nuclear tRNA 3'-end processing
-
physiological function
-
trz1 is responsible for the 3'-end processing of tRNA precursors, which is one of the essential steps in tRNA maturation. Trz1 is involved in nuclear tRNA 3'-end processing
-
physiological function
-
Schizosaccharomyces pombe has two tRNase Z genes, trz1 and trz2, required for nuclear and mitochondrial tRNA 3'-end processing, respectively. In addition, trz2 is also involved in generation of the 5'-ends of other mitochondrial RNAs, whose 5'-ends coincide with the 3'-end of tRNA
-
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D185G
dimerization, RNA binding, 7% activity compared to wild-type
D58A
dimerization, RNA binding, no activity
Deletion A252
dimerization, RNA binding, no activity
Delta200-212
weak dimerization, no RNA binding, no activity
Delta270-280
multimerization, no RNA binding, no activity
Delta49-164
weak dimerization, no RNA binding, no activity
Delta51-60
weak dimerization, no RNA binding, no activity
G184V
weak dimerization, no RNA binding, no activity
H133L
dimerization, weak RNA binding, no activity
H226L
dimerization, RNA binding, no activity
H248L
multimerization, no RNA binding, no activity
H54L
dimerization, weak RNA binding, no activity
H56L
weak dimerization, weak RNA binding, no activity
H59L
multimerization, no RNA binding, no activity
K203I
multimerization, no RNA binding, no activity
L205I
weak dimerization, RNA binding, 56% activity compared to wild-type
P83L
multimerization, no RNA binding, no activity
T186I
multimerization, no RNA binding, no activity
T210I
weak dimerization, RNA binding, 85% activity compared to wild-type
Y140L
weak dimerization, RNA binding, 30% activity compared to wild-type
Y253S
dimerization, RNA binding, 23% activity compared to wild-type
D211A
-
Asp(II), active site residue
D67A
-
Asp(I), active site residue
H140A
-
His(IV), active site residue
H247A
-
His(V), active site residue
H269A
-
His(VI), active site residue
H63A
-
His(I), active site residue
H68A
-
His(III), active site residue
A493T
processing efficiency similar to wild-type tRNase Z
A501T
processing efficiency similar to wild-type tRNase Z
A631T
HEAT-domain-variant
C442A
12fold reduction of processing efficiency compared to wild-type
C467A
8fold reduction of processing efficiency compared to wild-type
D466A
1500fold reduction of processing efficiency compared to wild-type
D502T
processing efficiency reduced 7420fold compared to wild-type tRNase Z
DELTAFA
deletion of the flexible arm (FA) hand close to its boundaries with the stalk does not interfere with stability and expression of tRNase ZL. DELTAFA hand variant has a Km ca. 100times higher and a kcat ca. 2times lower than wild-type tRNase Z
E469A
300fold reduction of processing efficiency compared to wild-type
E630A
HEAT-domain-variant
G196A/Pro201A
increases in Km as compared to wild-type tRNase Z
G200A
significant reductions in kcat as compared to wild-type tRNase Z
G209A
increases in Km as compared to wild-type tRNase Z
G438A
5000fold reduction of processing efficiency compared to wild-type
G440A
4fold reduction of processing efficiency compared to wild-type
G468A
900fold reduction of processing efficiency compared to wild-type
G470A
13fold reduction of processing efficiency compared to wild-type
G473A
8fold reduction of processing efficiency compared to wild-type
G480A
8fold reduction of processing efficiency compared to wild-type
G506A
processing efficiency reduced 11fold compared to wild-type tRNase Z
H498A
processing efficiency reduced 1950fold compared to wild-type tRNase Z
H500A
processing efficiency reduced 3379fold compared to wild-type tRNase Z
H503A
processing efficiency reduced 817fold compared to wild-type tRNase Z
H504A
processing efficiency reduced 7fold compared to wild-type tRNase Z
H629A
HEAT-domain-variant
I212A
increases in Km as compared to wild-type tRNase Z
I443A
8fold reduction of processing efficiency compared to wild-type
I475A
5fold reduction of processing efficiency compared to wild-type
I494A
processing efficiency similar to wild-type tRNase Z
I505A
processing efficiency similar to wild-type tRNase Z
I508A
processing efficiency reduced 6fold compared to wild-type tRNase Z
K214A/Lys218A
significant reductions in kcat as compared to wild-type tRNase Z
K446A
25fold reduction of processing efficiency compared to wild-type
L187A
substitution of alanine causes Km to increase almost as much as deletion of the entire flexible arm hand, with barely any decrease in kcat. A higher concentration of L187A enzyme than that of wild-type tRNase Z has to be used to accommodate the lower catalytic efficiency of the variant
L206A
increases in Km as compared to wild-type tRNase Z
L437A
7fold reduction of processing efficiency compared to wild-type
L464A
5fold reduction of processing efficiency compared to wild-type
L465A
10fold reduction of processing efficiency compared to wild-type
L478A
11fold reduction of processing efficiency compared to wild-type
L491A
processing efficiency reduced 7fold compared to wild-type tRNase Z
L499A
processing efficiency similar to wild-type tRNase Z
L507A
processing efficiency reduced 6fold compared to wild-type tRNase Z
N445A
5fold reduction of processing efficiency compared to wild-type
N449A
80fold reduction of processing efficiency compared to wild-type
P444A
5fold reduction of processing efficiency compared to wild-type
Q474A
750fold reduction of processing efficiency compared to wild-type
Q492A
processing efficiency similar to wild-type tRNase Z
R448A
625fold reduction of processing efficiency compared to wild-type
R477A
2600fold reduction of processing efficiency compared to wild-type
S441A
9fold reduction of processing efficiency compared to wild-type
S497A
processing efficiency reduced 495fold compared to wild-type tRNase Z
T439A
2.5fold reduction of processing efficiency compared to wild-type
T447A
2fold reduction of processing efficiency compared to wild-type
T471A
5fold reduction of processing efficiency compared to wild-type
T632A
HEAT-domain-variant
V450A
4fold reduction of processing efficiency compared to wild-type
V463A
6fold reduction of processing efficiency compared to wild-type
V476A
6fold reduction of processing efficiency compared to wild-type
V496A
processing efficiency similar to wild-type tRNase Z
Y472A
4fold reduction of processing efficiency compared to wild-type
Y479A
7fold reduction of processing efficiency compared to wild-type
Y495A
processing efficiency similar to wild-type tRNase Z
D212A
-
Asp(II) active site residue
D68A
-
Asp(I), active site residue
H141A
-
His(IV), active site residue
H248A
-
His(V), active site residue
H270A
-
His(VI), active site residue
H64A
-
His(I), active site residue
H66A
-
His(II), active site residue
H69A
-
His(III), active site residue
Q44S/Q46T
-
double mutant, cleavage of human pre-tRNA(Arg) after U75, very inefficiently
1641insG
-
frameshift mutation of ELAC2, lacks the C-terminal half, cannot increase suppression of ade6-704 in strain yYH1
D515A
-
tested for activity in presence of Mg2+ or Mn2+
D550A
-
Asp(I), active site residue
D666A
-
Asp(II), active site residue
E518A
-
tested for activity in presence of Mg2+ or Mn2+
E89A
-
influence on activity tested
F109S
-
influence on activity tested
G120Y
-
influence on activity tested
G281Y
-
influence on activity tested
G554L
-
tested for activity in presence of Mg2+ or Mn2+
H548A
-
His(II), active site residue
H551A
-
His(III), active site residue
H685A
-
tested for activity in presence of Mg2+ or Mn2+
H702A
-
His(V), active site residue
H724A
-
His(VI), active site residue
K282A
-
influence on activity tested
L539A
-
tested for activity in presence of Mg2+ or Mn2+
P493A
-
tested for activity in presence of Mg2+ or Mn2+
R497A
-
tested for activity in presence of Mg2+ or Mn2+
R718H
-
seems to be associated with the occurrence of prostate cancer
R781H
-
overexpression of this missense mutant of ELAC2 can increase suppression of ade6-704 in strain yYH1
T520Q
-
tested for activity in presence of Mg2+ or Mn2+
D476A
overexpression of Trz2 in yYH1 cells does not result in an increase in nonsense suppression by tRNASer(UGA)-M1
D578A
overexpression in yYH1 cells does not result in an increase in nonsense suppression by tRNASer(UGA)-M1
H574A
overexpression in yYH1 cells does not result in an increase in nonsense suppression by tRNASer(UGA)-M1
I572K
inactivates the protein
Y571L
mutation does not result in a temperature-sensitive phenotype
Q45S/Q47T
-
very low activity
D190A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
D25A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
D52A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
F11P
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
H134A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
H222A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
H244A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
H48A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
H50A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
H53A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
K162L
-
residue at the flexible arm of tRNase Z
K162L/R166L/K169L
-
residues at the flexible arm of tRNase Z
K162R
-
residue at the flexible arm of tRNase Z
K169L
-
residue at the flexible arm of tRNase Z
K169R
-
residue at the flexible arm of tRNase Z
R166L
-
residue at the flexible arm of tRNase Z
S31Q
-
cleavage site selection affected
S31Q/T33Q
-
cleavage site analyzed
T33Q
-
cleavage site selection affected
C25G
dimerization, RNA binding, 33% activity compared to wild-type
C25G
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
C40G
dimerization, RNA binding, similar activity compared to wild-type
C40G
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
E208A
dimerization, RNA binding, 55% activity compared to wild-type
E208A
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
F51L
dimerization, RNA binding, similar activity compared to wild-type
F51L
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
G62V
dimerization, RNA binding, 26% activity compared to wild-type
G62V
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
P178A
dimerization, RNA binding, 74% activity compared to wild-type
P178A
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
P64A
dimerization, RNA binding, similar activity compared to wild-type
P64A
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
R252G
dimerization, RNA binding, 26% activity compared to wild-type
R252G
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
H65A
the mutation was introduced at the central histidine to slow down hydrolysis of precursor tRNA during cocrystallization
H65A
-
His(II), active site residue
K207A
increases in Km as compared to wild-type tRNase Z
K207A
significant reductions in kcat as compared to wild-type tRNase Z
A541T
-
seems to be associated with the occurrence of prostate cancer
A541T
-
overexpression of this missense mutant of ELAC2 can increase suppression of ade6-704 in strain yYH1
H546A
-
His(I), active site residue
H546A
-
ELAC2 mutation, cannot increase suppression of ade6-704 in strain yYH1
S217L
-
seems to be associated with the occurrence of prostate cancer
S217L
-
overexpression of this missense mutant of ELAC2 can increase suppression of ade6-704 in strain yYH1
additional information
-
variants of tRNase Z enzymes generated by mutagenesis and properties of variants reviewed
additional information
Ala-scanning mutagenesis through five conserved loops on the carboxy side of motif II (motifs III, IV, HEAT,HST, and motif V) performed, pre-tRNA processing kinetics of the expressed variants studied
additional information
a conserved leucine at the ascending stalk/hand boundary causes practically the same increase in Km as the hand deletion, thus nearly eliminating its ability to bind substrate. Km also increases with substitutions in theGP(alpha4-alpha5) loop and at other conserved residues in the flexible arm hand predicted to contact substrate. Substitutions that reduce kcat are clustered in the beta10-beta11 loop
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Mayer, M.; Schiffer, S.; Marchfelder, A.
tRNA 3' processing in plants: nuclear and mitochondrial activities differ
Biochemistry
39
2096-2105
2000
Solanum tuberosum, Triticum aestivum
brenda
Nashimoto, M.; Tamura, M.; Kaspar, R.L.
Minimum requirements for substrates of mammalian tRNA 3' processing endoribonuclease
Biochemistry
38
12089-12096
1999
Sus scrofa
brenda
Nashimoto, M.
Distribution of both lengths and 5' terminal nucleotides of mammalian pre-tRNA 3' trailers reflects properties of 3' processing endoribonuclease
Nucleic Acids Res.
25
1148-1154
1997
Homo sapiens, Mus musculus, Sus scrofa
brenda
Nashimoto, M.; Geary, S.; Tamura, M.; Kaspar, R.
RNA heptamers that direct RNA cleavage by mammalian tRNA 3' processing endoribonuclease
Nucleic Acids Res.
26
2565-2571
1998
Mus musculus, Sus scrofa
brenda
Nashimoto, M.; Wesemann, D.R.; Geary, S.; Tamura, M.; Kaspar, R.L.
Long 5' leaders inhibit removal of a 3' trailer from a precursor tRNA by mammalian tRNA 3' processing endoribonuclease
Nucleic Acids Res.
27
2770-2776
1999
Sus scrofa
brenda
Han, S.J.; Kang, H.S.
Purification and characterization of the precursor tRNA 3'-end processing nuclease from Aspergillus nidulans
Biochem. Biophys. Res. Commun.
233
354-358
1997
Aspergillus nidulans
brenda
Mrl, M.; Marchfelder, A.
The final cut. The importance of tRNA 3'-processing
EMBO Rep.
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17-20
2001
Saccharomyces cerevisiae, Homo sapiens, Physarum sp., Rattus norvegicus
brenda
Mohan, A.; Whyte, S.; Wang, X.; Nashimoto, M.; Levinger, L.
The 3' end CCA of mature tRNA is an antideterminant for eukaryotic 3' -tRNase
RNA
5
245-256
1999
Drosophila melanogaster, Sus scrofa
brenda
Oommen, A.; Li, X.; Gegenheimer, P.
Cleavage specificity of chloroplast and nuclear tRNA 3'-processing nucleases
Mol. Cell. Biol.
12
865-875
1992
Saccharomyces cerevisiae, Spinacia oleracea, Triticum aestivum
brenda
Nashimoto, M.
Anomalous RNA substrates for mammalian tRNA 3' processing endoribonuclease
FEBS Lett.
472
179-186
2000
Sus scrofa
brenda
Nashimoto, M.; Tamura, M.; Kaspar, R.L.
Selection of cleavage site by mammalian tRNA 3' processing endoribonuclease
J. Mol. Biol.
287
727-740
1999
Sus scrofa
brenda
Schierling, K.; Roesch, S.; Rupprecht, R.; Schiffer, S.; Marchfelder, A.
tRNA 3' end maturation in archaea has eukaryotic features: the RNase Z from Haloferax volcanii
J. Mol. Biol.
316
895-902
2002
Haloferax volcanii, Rattus norvegicus, Solanum tuberosum, Triticum aestivum, Xenopus laevis
brenda
Kunzmann, A.; Brennicke, A.; Marchfelder, A.
5' End maturation and RNA editing have to precede tRNA 3' processing in plant mitochondria
Proc. Natl. Acad. Sci. USA
95
108-113
1998
Solanum tuberosum
brenda
Kruszka, K.; Barneche, F.; Guyot, R.; Ailhas, J.; Meneau, I.; Schiffer, S.; Marchfelder, A.; Echeverria, M.
Plant dicistronic tRNA-snoRNA genes: a new mode of expression of the small nucleolar RNAs processed by RNase Z
EMBO J.
22
621-632
2003
Arabidopsis thaliana, Rattus norvegicus
brenda
Manam, S.; Van Tuyle, G.C.
Separation and characterization of 5'- and 3'-tRNA processing nucleases from rat liver mitochondria
J. Biol. Chem.
262
10272-10279
1987
Rattus norvegicus
brenda
Schiffer, S.; Rsch, S.; Marchfelder, A.
Assigning a function to a conserved group of proteins: the tRNA 3'-processing enzymes
EMBO J.
21
2769-2777
2002
Arabidopsis thaliana, Methanocaldococcus jannaschii (Q58897), Triticum aestivum (P60193), Triticum aestivum
brenda
Schiffer, S.; Helm, M.; Theobald-Dietrich, A.; Giege, R.; Marchfelder, A.
The plant tRNA 3' processing enzyme has a broad substrate spectrum
Biochemistry
40
8264-8272
2001
Solanum tuberosum
brenda
Shibata, H.S.; Minagawa, A.; Takaku, H.; Takagi, M.; Nashimoto, M.
Unstructured RNA is a substrate for tRNase Z
Biochemistry
45
5486-5492
2006
Bacillus subtilis, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Pyrobaculum aerophilum, Sus scrofa, Thermotoga maritima
brenda
Schiffer, S.; Rosch, S.; Marchfelder, A.
Recombinant RNase Z does not recognize CCA as part of the tRNA and its cleavage efficiency is influenced by acceptor stem length
Biol. Chem.
384
333-342
2003
Arabidopsis thaliana, Methanocaldococcus jannaschii, Triticum aestivum
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The tRNase Z family of proteins: physiological functions, substrate specificity and structural properties
Biol. Chem.
386
1253-1264
2005
Arabidopsis thaliana, Arabidopsis thaliana (Q8L633), Arabidopsis thaliana (Q8LGU7), Arabidopsis thaliana (Q8VYS2), Haloferax volcanii, Thermotoga maritima, Caenorhabditis elegans (O44476), Escherichia coli (P0A8V0), Saccharomyces cerevisiae (P36159), Bacillus subtilis (P54548), Methanocaldococcus jannaschii (Q58897), Drosophila melanogaster (Q8MKW7), Pyrococcus furiosus (Q8U182), Pyrobaculum aerophilum (Q8ZTJ7), Homo sapiens (Q9BQ52), Homo sapiens (Q9H777), Thermoplasma acidophilum (Q9HJ19)
brenda
Pellegrini, O.; Nezzar, J.; Marchfelder, A.; Putzer, H.; Condon, C.
Endonucleolytic processing of CCA-less tRNA precursors by RNase Z in Bacillus subtilis
EMBO J.
22
4534-4543
2003
Bacillus subtilis
brenda
Kostelecky, B.; Pohl, E.; Vogel, A.; Schilling, O.; Meyer-Klaucke, W.
The crystal structure of the zinc phosphodiesterase from Escherichia coli provides insight into function and cooperativity of tRNase Z-family proteins
J. Bacteriol.
188
1607-1614
2006
Escherichia coli
brenda
Ishii, R.; Minagawa, A.; Takaku, H.; Takagi, M.; Nashimoto, M.; Yokoyama, S.
Crystal structure of the tRNA 3' processing endoribonuclease tRNase Z from Thermotoga maritima
J. Biol. Chem.
280
14138-14144
2005
Thermotoga maritima
brenda
Ceballos-Chavez, M.; Vioque, A.
Sequence-dependent cleavage site selection by RNase Z from the cyanobacterium Synechocystis sp. PCC 6803
J. Biol. Chem.
280
33461-33469
2005
Synechocystis sp.
brenda
Spath, B.; Kirchner, S.; Vogel, A.; Schubert, S.; Meinlschmidt, P.; Aymanns, S.; Nezzar, J.; Marchfelder, A.
Analysis of the functional modules of the tRNA 3' endonuclease (tRNase Z)
J. Biol. Chem.
280
35440-35447
2005
Arabidopsis thaliana (Q8LGU7)
brenda
Yan, H.; Zareen, N.; Levinger, L.
Naturally occurring mutations in human mitochondrial pre-tRNASer(UCN) can affect the transfer ribonuclease Z cleavage site, processing kinetics, and substrate secondary structure
J. Biol. Chem.
281
3926-3935
2006
Homo sapiens
brenda
Zareen, N.; Yan, H.; Hopkinson, A.; Levinger, L.
Residues in the conserved His domain of fruit fly tRNase Z that function in catalysis are not involved in substrate recognition or binding
J. Mol. Biol.
350
189-199
2005
Drosophila melanogaster (Q8MKW7)
brenda
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Structure of the ubiquitous 3' processing enzyme RNase Z bound to transfer RNA
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Drosophila melanogaster (Q8MKW7)
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Zareen, N.; Hopkinson, A.; Levinger, L.
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Drosophila melanogaster (Q8MKW7)
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Ishii, R.; Minagawa, A.; Takaku, H.; Takagi, M.; Nashimoto, M.; Yokoyama, S.
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Thermotoga maritima
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Metal requirements and phosphodiesterase activity of tRNase Z enzymes
Biochemistry
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Arabidopsis thaliana, Drosophila melanogaster, Saccharomyces cerevisiae (P36159)
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Karkashon, S.; Hopkinson, A.; Levinger, L.
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Drosophila melanogaster (Q8MKW7)
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Spaeth, B.; Canino, G.; Marchfelder, A.
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Arabidopsis thaliana, Caenorhabditis elegans, Danio rerio, Drosophila melanogaster (Q8MKW7), Gallus gallus, Homo sapiens, Mus musculus, Neurospora crassa, Saccharomyces cerevisiae, Schizosaccharomyces pombe
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Escherichia coli, Homo sapiens
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Aspergillus nidulans, Bacteroides fragilis, Bombyx mori, Bradyrhizobium japonicum, Saccharomyces cerevisiae, Caenorhabditis elegans, Chlamydia trachomatis, Clostridium acetobutylicum, Clostridium spp., Deinococcus radiodurans, Streptococcus pneumoniae, Drosophila melanogaster, Escherichia coli, Lacticaseibacillus casei, Listeria monocytogenes, Methanocaldococcus jannaschii, Staphylococcus aureus, Mycobacterium tuberculosis, Myxococcus xanthus, Prochlorococcus marinus, Streptomyces coelicolor, Saccharolobus solfataricus, Thermotoga maritima, Treponema pallidum, Xenopus laevis, Nanoarchaeum equitans, Methanococcoides burtonii, Haloquadratum walsbyi, Bacillus subtilis (P54548)
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Escherichia coli tRNase Z can shut down growth probably by removing amino acids from aminoacyl-tRNAs
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Escherichia coli
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Arabidopsis thaliana, Arabidopsis thaliana (Q8L633), Arabidopsis thaliana (Q8LGU7)
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PLoS ONE
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Bombyx mori, Danio rerio, Branchiostoma floridae, Caenorhabditis elegans, Canis lupus familiaris, Ciona intestinalis, Drosophila melanogaster, Homo sapiens, Hydra vulgaris, Mus musculus, Salmo salar, Strongylocentrotus purpuratus, Tribolium castaneum, Monosiga brevicollis, Xenopus tropicalis, Loxodonta africana, Lottia gigantea, Nematostella vectensis, Capitella teleta, Amphimedon queenslandica, Trichoplax adhaerens
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Tethered domains and flexible regions in tRNase Z(L), the long form of tRNase Z
PLoS ONE
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Drosophila melanogaster, Homo sapiens
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Ma, M.; Li de la Sierra-Gallay, I.; Lazar, N.; Pellegrini, O.; Lepault, J.; Condon, C.; Durand, D.; van Tilbeurgh, H.
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Saccharomyces cerevisiae (P36159), Saccharomyces cerevisiae
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Mus musculus (Q80Y81)
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Schizosaccharomyces pombe (P87168), Schizosaccharomyces pombe, Schizosaccharomyces pombe ATCC 24843 (P87168)
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Characterization of cis-elements in the promoter of trz2 encoding Schizosaccharomyces pombe mitochondrial tRNA 3'-end processing enzyme
Microbiology
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Schizosaccharomyces pombe (P87168), Schizosaccharomyces pombe (Q10155), Schizosaccharomyces pombe, Schizosaccharomyces pombe ATCC 24843 (P87168), Schizosaccharomyces pombe ATCC 24843 (Q10155)
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Ma, M.; Li de la Sierra-Gallay, I.; Lazar, N.; Pellegrini, O.; Durand, D.; Marchfelder, A.; Condon, C.; van Tilbeurgh, H.
The crystal structure of Trz1, the long form RNase Z from yeast
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Saccharomyces cerevisiae (P36159), Saccharomyces cerevisiae
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Ninomiya, S.; Kawano, M.; Abe, T.; Ishikawa, T.; Takahashi, M.; Tamura, M.; Takahashi, Y.; Nashimoto, M.
Potential small guide RNAs for tRNase ZL from human plasma, peripheral blood mononuclear cells, and cultured cell lines
PLoS ONE
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Homo sapiens
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Saoura, M.; Pinnock, K.; Pujantell-Graell, M.; Levinger, L.
Substitutions in conserved regions preceding and within the linker affect activity and flexibility of tRNase ZL, the long form of tRNase Z
PLoS ONE
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Drosophila melanogaster (Q8MKW7), Drosophila melanogaster
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