Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + adenine32 in tRNAPro(GGG)
S-adenosyl-L-homocysteine + 2'-O-methyladenine32 in tRNAPro(GGG)
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
S-adenosyl-L-methionine + cytidine32 in tRNAMet(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylcytisine32 in tRNA
S-adenosyl-L-methionine + cytidine32 in tRNATrp(CCA)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNATrp(CCA)
S-adenosyl-L-methionine + nucleoside32 in EctRNAfMet1(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAfMet1(CAU)
S-adenosyl-L-methionine + nucleoside32 in EctRNAfMet2(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAfMet2(CAU)
S-adenosyl-L-methionine + nucleoside32 in EctRNAGln1(UUG)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAGln1(UUG)
S-adenosyl-L-methionine + nucleoside32 in EctRNAGln2(CUG)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAGln2(CUG)
-
-
-
?
S-adenosyl-L-methionine + nucleoside32 in EctRNASer1(UGA)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNASer1(UGA)
-
-
-
?
S-adenosyl-L-methionine + nucleoside32 in EctRNATrp1(CCA)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNATrp1(CCA)
-
-
-
?
S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
S-adenosyl-L-methionine + uridine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNA
S-adenosyl-L-methionine + uridine32 in tRNAGln(UUG)
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNAGln(UUG)
-
-
-
?
S-adenosyl-L-methionine + uridine32 in tRNAPro(CGG)
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNAPro(CGG)
-
-
-
?
S-adenosyl-L-methionine + uridine32 in tRNAPro(UGG)
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNAPro(UGG)
-
-
-
?
additional information
?
-
S-adenosyl-L-methionine + adenine32 in tRNAPro(GGG)
S-adenosyl-L-homocysteine + 2'-O-methyladenine32 in tRNAPro(GGG)
tRNAPro(GGG) is the most efficient substrate, with methyladenine formation an order of magnitude higher than methyluridine or methylcytidine in other substrates
-
-
?
S-adenosyl-L-methionine + adenine32 in tRNAPro(GGG)
S-adenosyl-L-homocysteine + 2'-O-methyladenine32 in tRNAPro(GGG)
tRNAPro(GGG) is the most efficient substrate, with methyladenine formation an order of magnitude higher than methyluridine or methylcytidine in other substrates
-
-
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
presence of 2'-O-methylated cytidine at position 32 in tRNAfMet1(CAU), tRNAfMet2(CAU), tRNASer1(UGA), and tRNATrp1(CCA). In Escherichia coli YfhQ is the only methyltransferase responsible for the formation of Cm32 in tRNA
-
-
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
2'-O-methylation of cytidine34 in tRNAGln2(CUG). Total crude tRNA extracted from the wild-type strain MC1061 was not a substrate for the purified YfhQ enzyme, while tRNA from the yfhQ K.O. strain is an excellent substrate for this enzyme
-
-
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
-
-
-
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
-
-
-
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
while the four canonical nucleosides are substrates of the Escherichia coli enzyme at position 32 of tRNA, the archaeal TrmJ can only methylate the ribose of a cytidine
-
-
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
while the four canonical nucleosides are substrates of the Escherichia coli enzyme at position 32 of tRNA, the archaeal TrmJ can only methylate the ribose of a cytidine
-
-
?
S-adenosyl-L-methionine + cytidine32 in tRNAMet(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylcytisine32 in tRNA
-
-
-
?
S-adenosyl-L-methionine + cytidine32 in tRNAMet(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylcytisine32 in tRNA
-
-
-
?
S-adenosyl-L-methionine + cytidine32 in tRNATrp(CCA)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNATrp(CCA)
-
-
-
?
S-adenosyl-L-methionine + cytidine32 in tRNATrp(CCA)
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNATrp(CCA)
-
-
-
?
S-adenosyl-L-methionine + nucleoside32 in EctRNAfMet1(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAfMet1(CAU)
-
-
-
?
S-adenosyl-L-methionine + nucleoside32 in EctRNAfMet1(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAfMet1(CAU)
-
-
-
?
S-adenosyl-L-methionine + nucleoside32 in EctRNAfMet2(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAfMet2(CAU)
-
-
-
?
S-adenosyl-L-methionine + nucleoside32 in EctRNAfMet2(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAfMet2(CAU)
-
-
-
?
S-adenosyl-L-methionine + nucleoside32 in EctRNAGln1(UUG)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAGln1(UUG)
-
-
-
?
S-adenosyl-L-methionine + nucleoside32 in EctRNAGln1(UUG)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAGln1(UUG)
-
-
-
?
S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
-
-
-
?
S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
-
-
-
?
S-adenosyl-L-methionine + uridine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNA
presence of 2'-O-methylated uridine in position 32 of the anticodon loop in tRNAGln1(UUG) and tRNAGln2(CUG)
-
-
?
S-adenosyl-L-methionine + uridine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNA
2'-O-methylation of uridine34 tRNASer1(UGA). Total crude tRNA extracted from the wild-type strain MC1061 was not a substrate for the purified YfhQ enzyme, while tRNA from the yfhQ K.O. strain is an excellent substrate for this enzyme
-
-
?
additional information
?
-
no methylation of cytosine 34 in tRNALeu(CAA)
-
-
?
additional information
?
-
-
no methylation of cytosine 34 in tRNALeu(CAA)
-
-
?
additional information
?
-
bacterial TrmJs recognize substrate tRNAs and specifically catalyze a 2'-O modification at ribose 32. All six Escherichia coli tRNAs with 2'-O-methylated nucleosides at position 32 are substrates of EcTrmJ. The elbow region of tRNA, but not the amino acid acceptor stem, is needed for the methylation reaction. tRNA recognition by EcTrmJ involves the cooperative influences of conserved residues from both the SPOUT and extensional domains, and this process is regulated by the flexible hinge region that connects these two domains
-
-
?
additional information
?
-
bacterial TrmJs recognize substrate tRNAs and specifically catalyze a 2'-O modification at ribose 32. All six Escherichia coli tRNAs with 2'-O-methylated nucleosides at position 32 are substrates of EcTrmJ. The elbow region of tRNA, but not the amino acid acceptor stem, is needed for the methylation reaction. tRNA recognition by EcTrmJ involves the cooperative influences of conserved residues from both the SPOUT and extensional domains, and this process is regulated by the flexible hinge region that connects these two domains
-
-
?
additional information
?
-
PA14 TrmJ catalyzes 2'-O-methylation of C, U and A at position 32 in the tRNA anticodon loop. tRNA substrates for reaction with PA14 TrmJ are prepared by in vitro T7 transcription. Substrate specificity, overview. No or poor activity with tRNASer(UGA) and tRNAHis(GUG). Structure analysis of TrmJ-NTD tRNA binding
-
-
-
additional information
?
-
PA14 TrmJ catalyzes 2'-O-methylation of C, U and A at position 32 in the tRNA anticodon loop. tRNA substrates for reaction with PA14 TrmJ are prepared by in vitro T7 transcription. Substrate specificity, overview. No or poor activity with tRNASer(UGA) and tRNAHis(GUG). Structure analysis of TrmJ-NTD tRNA binding
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
S-adenosyl-L-methionine + uridine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNA
presence of 2'-O-methylated uridine in position 32 of the anticodon loop in tRNAGln1(UUG) and tRNAGln2(CUG)
-
-
?
additional information
?
-
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
presence of 2'-O-methylated cytidine at position 32 in tRNAfMet1(CAU), tRNAfMet2(CAU), tRNASer1(UGA), and tRNATrp1(CCA). In Escherichia coli YfhQ is the only methyltransferase responsible for the formation of Cm32 in tRNA
-
-
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
-
-
-
?
S-adenosyl-L-methionine + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
-
-
-
?
S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
-
-
-
?
S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
-
-
-
?
additional information
?
-
bacterial TrmJs recognize substrate tRNAs and specifically catalyze a 2'-O modification at ribose 32. All six Escherichia coli tRNAs with 2'-O-methylated nucleosides at position 32 are substrates of EcTrmJ. The elbow region of tRNA, but not the amino acid acceptor stem, is needed for the methylation reaction. tRNA recognition by EcTrmJ involves the cooperative influences of conserved residues from both the SPOUT and extensional domains, and this process is regulated by the flexible hinge region that connects these two domains
-
-
?
additional information
?
-
bacterial TrmJs recognize substrate tRNAs and specifically catalyze a 2'-O modification at ribose 32. All six Escherichia coli tRNAs with 2'-O-methylated nucleosides at position 32 are substrates of EcTrmJ. The elbow region of tRNA, but not the amino acid acceptor stem, is needed for the methylation reaction. tRNA recognition by EcTrmJ involves the cooperative influences of conserved residues from both the SPOUT and extensional domains, and this process is regulated by the flexible hinge region that connects these two domains
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
TrmJ proteins from the SPOUT methyltransferase superfamily are tRNA Xm32 modification enzymes that occur in bacteria and archaea. Unlike archaeal TrmJ, bacterial TrmJ require full-length tRNA molecules as substrates
evolution
PA14 14690 possesses the conserved region of TrmJ-specific motif, a consensus TXARXR sequence (residues 79-84). This motif has been shown to be critical for binding of SAM/SAH and tRNA. PA14 14690 also contains a conserved Arg at position 23, which is proposed to be involved in its catalytic activity. Another catalytic residue, the Tyr at position 141, is replaced by Phe. In addition to Arg positions 82 and 84 in the TrmJ-specific motif, PA14 14690 also contains more key conserved tRNA binding residues including arginine at positions 100, 101 and 105
evolution
-
TrmJ proteins from the SPOUT methyltransferase superfamily are tRNA Xm32 modification enzymes that occur in bacteria and archaea. Unlike archaeal TrmJ, bacterial TrmJ require full-length tRNA molecules as substrates
-
evolution
-
PA14 14690 possesses the conserved region of TrmJ-specific motif, a consensus TXARXR sequence (residues 79-84). This motif has been shown to be critical for binding of SAM/SAH and tRNA. PA14 14690 also contains a conserved Arg at position 23, which is proposed to be involved in its catalytic activity. Another catalytic residue, the Tyr at position 141, is replaced by Phe. In addition to Arg positions 82 and 84 in the TrmJ-specific motif, PA14 14690 also contains more key conserved tRNA binding residues including arginine at positions 100, 101 and 105
-
malfunction
loss of trmJ causes an increased susceptibility to H2O2. Phenotypic analysis of cytotoxicity induced by H2O2 in PA14 wild-type strain, trmJ mutant strain, and the trmJ complementation strain or trmJC, overview. Inactivation of trmJ abolishes Cm, Um, or Am formation in Pseudomonas aeruginosa tRNA
malfunction
-
loss of trmJ causes an increased susceptibility to H2O2. Phenotypic analysis of cytotoxicity induced by H2O2 in PA14 wild-type strain, trmJ mutant strain, and the trmJ complementation strain or trmJC, overview. Inactivation of trmJ abolishes Cm, Um, or Am formation in Pseudomonas aeruginosa tRNA
-
metabolism
methylation at position 32 of tRNA catalyzed by TrmJ alters oxidative stress response in Pseudomonas aeruginosa
metabolism
-
methylation at position 32 of tRNA catalyzed by TrmJ alters oxidative stress response in Pseudomonas aeruginosa
-
physiological function
methylation of ribose moieties in tRNA is frequent, especially at position 32 where it is commonplace in all three domains of life
physiological function
PA14 trmJ encodes a tRNA (cytidine(32)/uridine(32)/adenosine(32)-2'-O)-methyltransferase that regulates the expression of oxidative stress response genes. Role of tRNA modifications in the oxidative stress response of prokaryotes. TrmJ is a tRNA:Cm32/Um32/Am32 methyltransferase involved in translational fidelity and the oxidative stress response. TrmJ confers H2O2 resistance in part by upregulating the expression of catalase genes
physiological function
-
methylation of ribose moieties in tRNA is frequent, especially at position 32 where it is commonplace in all three domains of life
-
physiological function
-
PA14 trmJ encodes a tRNA (cytidine(32)/uridine(32)/adenosine(32)-2'-O)-methyltransferase that regulates the expression of oxidative stress response genes. Role of tRNA modifications in the oxidative stress response of prokaryotes. TrmJ is a tRNA:Cm32/Um32/Am32 methyltransferase involved in translational fidelity and the oxidative stress response. TrmJ confers H2O2 resistance in part by upregulating the expression of catalase genes
-
additional information
semi-quantitative real-time PCR analysis of oxyR, katA, katB, katE, ankB and recG transcripts in response to H2O2. Analysis of ribonucleosides by HPLC-coupled tandem quadrupole mass spectrometry
additional information
-
semi-quantitative real-time PCR analysis of oxyR, katA, katB, katE, ankB and recG transcripts in response to H2O2. Analysis of ribonucleosides by HPLC-coupled tandem quadrupole mass spectrometry
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
purified recombinant C-terminally His6-tagged wild-type enzyme, hanging drop vapour diffusion method, mixing of 10 mg/ml of protein 20 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM MgCl2, and 2 mM S-adenosyl-L-homocysteine, with 3.6 M NaCl and 0.1 M HEPES, pH 8.2, 20°C, 2 months, X-ray diffraction structure determination and analysis, full-length EcTrmJ forms an unusual dimer in the asymmetric unit, with both the catalytic SPOUT domain and C-terminal extension forming separate dimeric associations in the crystal structure, molecular replacement
recombinant TrmJ-NTD protein, hanging drop vapour diffusion method, mixing of 0.001 ml of 20 mg/ml protein solution with 0.002 ml of reservoir solution containing Bis-Tris propane, pH 6.5, 0.2 M ammonium chloride, 25% w/v PEG 3350, 20°C, or with 0.03 M MgCl2, 0.03 M CaCl2, 20% w/v PEG MME550, 10% w/v PEG 20000, and 0.1 M MOPS/Na-HEPES, pH 7.5, and soaking with 1 mM sinefungin, 20°C, resulting in two different crystal forms, method optimization, X-ray diffraction structure determination and analysis at 1.7 A and 1.8-2.2 A resolution, respectively
crystal structure of the catalytic domain
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
E225A
site-directed mutagenesis, inactive mutant
F199A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
G231A
site-directed mutagenesis, inactive mutant
I228A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
L229A
site-directed mutagenesis, inactive mutant
E225A
-
site-directed mutagenesis, inactive mutant
-
F199A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
G231A
-
site-directed mutagenesis, inactive mutant
-
L229A
-
site-directed mutagenesis, inactive mutant
-
additional information
generation of several partial deletion mutants of TrmJ, including single site mutants, DELTA2 (deleted residues 171-172), DELTA4 (deleted residues 171-174), DELTA7 (deleted residues 169-175), DELTA10 (deleted residues 167-176), DELTA12 (deleted residues 166-177), NTD (residues 1-170) and CTD (residues 171-246)
additional information
-
generation of several partial deletion mutants of TrmJ, including single site mutants, DELTA2 (deleted residues 171-172), DELTA4 (deleted residues 171-174), DELTA7 (deleted residues 169-175), DELTA10 (deleted residues 167-176), DELTA12 (deleted residues 166-177), NTD (residues 1-170) and CTD (residues 171-246)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purta, E.; van Vliet, F.; Tkaczuk, K.L.; Dunin-Horkawicz, S.; Mori, H.; Droogmans, L.; Bujnicki, J.M.
The yfhQ gene of Escherichia coli encodes a tRNA:Cm32/Um32 methyltransferase
BMC Mol. Biol.
7
23
2006
Escherichia coli (P0AE01), Escherichia coli
brenda
Somme, J.; Van Laer, B.; Roovers, M.; Steyaert, J.; Versees, W.; Droogmans, L.
Characterization of two homologous 2'-O-methyltransferases showing different specificities for their tRNA substrates
RNA
20
1257-1271
2014
Sulfolobus acidocaldarius (Q4JB16), Sulfolobus acidocaldarius DSM 639 (Q4JB16)
brenda
Liu, R.J.; Long, T.; Zhou, M.; Zhou, X.L.; Wang, E.D.
tRNA recognition by a bacterial tRNA Xm32 modification enzyme from the SPOUT methyltransferase superfamily
Nucleic Acids Res.
43
7489-7503
2015
Escherichia coli (P0AE01), Escherichia coli K-12 MG1655 (P0AE01)
brenda
Jaroensuk, J.; Atichartpongkul, S.; Chionh, Y.; Hwa Wong, Y.; Liew, C.; McBee, M.; Thongdee, N.; Prestwich, E.; DeMott, M.; Mongkolsuk, S.; Dedon, P.; Lescar, J.; Fuangthong, M.
Methylation at position 32 of tRNA catalyzed by TrmJ alters oxidative stress response in Pseudomonas aeruginosa
Nucleic Acids Res.
44
10834-10848
2016
Pseudomonas aeruginosa (A0A0H2ZF87), Pseudomonas aeruginosa UCBPP-PA14 (A0A0H2ZF87)
brenda