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tRNA-C-C-A-C2 + phosphate
?
-
-
-
-
?
tRNA-C-C-A-C3 + phosphate
?
-
-
-
-
?
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
additional information
?
-
poly(A) + phosphate
?
-
-
-
-
r
poly(A) + phosphate
?
-
phosphorolysis of poly(A) 15times more rapidly than of tRNA-C-C-A-Cn
-
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
-
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
-
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
substrate specificity
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
dependent on phosphate
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
dependent on phosphate
enzyme can utilize all dinucleotides as substrates for the reverse reaction
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
phosphorolysis of poly(A) 15times more rapidly than of tRNA-C-C-A-Cn
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
tRNA-C-C-A-Cn
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
tRNA-C-C-A-Cn
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
reverse reaction is synthetic
-
ir
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
brings about the final exonucleolytic trimming of the 3'-terminus of tRNA precursors in E. coli by phosphorolysis, producing a mature 3'-terminus on tRNA and nucleoside diphosphate
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
brings about the final exonucleolytic trimming of the 3'-terminus of tRNA precursors in E. coli by phosphorolysis, producing a mature 3'-terminus on tRNA and nucleoside diphosphate
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
brings about the final exonucleolytic trimming of the 3'-terminus of tRNA precursors in E. coli by phosphorolysis, producing a mature 3'-terminus on tRNA and nucleoside diphosphate
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
implicated in the 3'-processing of tRNA precursors
-
ir
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
implicated in the 3'-processing of tRNA precursors
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
role in tRNA processing and RNA degradation
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
-
-
?
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
implicated in the 3'-processing of tRNA precursors
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
-
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
involved in the maturation of tRNA precursors and especially important for removal of nucleotide residues near the CCA acceptor end of the mature tRNAs
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
plays a major role in the exonucleolytic maturation of CCA-containing tRNA precursors, degradation of the last few nucleotides before the acceptor stem
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
degradation of 16S rRNA substrate 3' end
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
the enzyme is a 3' to 5' RNase. The enzyme digests through RNA duplexes of moderate stability
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
16S rRNA substrate
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
the enzyme is a 3' to 5' RNase. RNase PH uses phosphate as a nucleophile to catalyze RNA cleavage
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
the enzyme is a 3' to 5' RNase. The enzyme digests through RNA duplexes of moderate stability
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
the enzyme is a 3' to 5' RNase. RNase PH uses phosphate as a nucleophile to catalyze RNA cleavage
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
degradation of 16S rRNA substrate 3' end
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
16S rRNA substrate
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
-
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
catalyzes the removal of nucleotides at the 3' end of the tRNA precursor, leading to the release of nucleoside diphosphate, and generates the CCA end during the maturation process
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
-
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
-
-
-
?
additional information
?
-
-
phosphate-dependent tRNA nucleotidyltransferase and polynucleotide phosphorylase activity play an essential role that affects ribosome metabolism, this function cannot be taken over by any of the hydrolytic exonucleases present in the cell
-
-
?
additional information
?
-
-
for 16S rRNA degradation during glucose starvation, leading to slow cell growth, begins with shortening of its 3' end in a reaction catalyzed by RNase PH
-
-
?
additional information
?
-
-
for 16S rRNA degradation during glucose starvation, leading to slow cell growth, begins with shortening of its 3' end in a reaction catalyzed by RNase PH
-
-
?
additional information
?
-
-
the reaction proceeds via strongly bound phosphate ions in the phosphorolytic active sites of mthRrp41 protein
-
-
?
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tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
additional information
?
-
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
reverse reaction is synthetic
-
ir
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
brings about the final exonucleolytic trimming of the 3'-terminus of tRNA precursors in E. coli by phosphorolysis, producing a mature 3'-terminus on tRNA and nucleoside diphosphate
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
brings about the final exonucleolytic trimming of the 3'-terminus of tRNA precursors in E. coli by phosphorolysis, producing a mature 3'-terminus on tRNA and nucleoside diphosphate
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
brings about the final exonucleolytic trimming of the 3'-terminus of tRNA precursors in E. coli by phosphorolysis, producing a mature 3'-terminus on tRNA and nucleoside diphosphate
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
implicated in the 3'-processing of tRNA precursors
-
ir
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
implicated in the 3'-processing of tRNA precursors
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
role in tRNA processing and RNA degradation
-
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
implicated in the 3'-processing of tRNA precursors
-
r
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
involved in the maturation of tRNA precursors and especially important for removal of nucleotide residues near the CCA acceptor end of the mature tRNAs
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
plays a major role in the exonucleolytic maturation of CCA-containing tRNA precursors, degradation of the last few nucleotides before the acceptor stem
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
degradation of 16S rRNA substrate 3' end
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
the enzyme is a 3' to 5' RNase. The enzyme digests through RNA duplexes of moderate stability
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
the enzyme is a 3' to 5' RNase. The enzyme digests through RNA duplexes of moderate stability
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
degradation of 16S rRNA substrate 3' end
-
-
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
catalyzes the removal of nucleotides at the 3' end of the tRNA precursor, leading to the release of nucleoside diphosphate, and generates the CCA end during the maturation process
-
-
?
additional information
?
-
-
phosphate-dependent tRNA nucleotidyltransferase and polynucleotide phosphorylase activity play an essential role that affects ribosome metabolism, this function cannot be taken over by any of the hydrolytic exonucleases present in the cell
-
-
?
additional information
?
-
-
for 16S rRNA degradation during glucose starvation, leading to slow cell growth, begins with shortening of its 3' end in a reaction catalyzed by RNase PH
-
-
?
additional information
?
-
-
for 16S rRNA degradation during glucose starvation, leading to slow cell growth, begins with shortening of its 3' end in a reaction catalyzed by RNase PH
-
-
?
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Anemia, Sideroblastic
In vitro studies of disease-linked variants of human tRNA nucleotidyltransferase reveal decreased thermal stability and altered catalytic activity.
Carcinoma, Ehrlich Tumor
Effect of nucleoside 5'-triphosphates on tRNA nucleotidyltransferase activity in cytoplasmic fractions of various types of mammalian cells.
Carcinoma, Ehrlich Tumor
Possible regulation by nucleosidediphosphate kinase involvement of the synthesis of tRNA 3'-terminal -pCpCpA in mammalian cells.
Hypersensitivity
Functions that protect Escherichia coli from DNA-protein crosslinks.
Infections
A physiological role for tRNA nucleotidyltransferase during bacteriophage infection.
Melanoma
Defining the domains of human polynucleotide phosphorylase (hPNPaseOLD-35) mediating cellular senescence.
Neoplasms
A unique T-cell monoclonal antibody with potential uses in autologous bone marrow transplantation.
Neoplasms
Effect of nucleoside 5'-triphosphates on tRNA nucleotidyltransferase activity in cytoplasmic fractions of various types of mammalian cells.
Neoplasms
Identification of a tRNA nucleotidyltransferase and its substrates in virions of avian RNA tumor viruses.
Neoplasms
Possible regulation by nucleosidediphosphate kinase involvement of the synthesis of tRNA 3'-terminal -pCpCpA in mammalian cells.
Retinitis Pigmentosa
In vitro studies of disease-linked variants of human tRNA nucleotidyltransferase reveal decreased thermal stability and altered catalytic activity.
Starvation
Degradation of ribosomal RNA during starvation: comparison to quality control during steady-state growth and a role for RNase PH.
Starvation
Elucidation of pathways of ribosomal RNA degradation: an essential role for RNase E.
Starvation
Physiological studies of Escherichia coli strain MG1655: growth defects and apparent cross-regulation of gene expression.
Starvation
RNase II regulates RNase PH and is essential for cell survival during starvation and stationary phase.
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additional information
-
the core of the exosome is a versatile multisubunit RNA processing enzyme found in archaea and eukaryotes, which includes a ring of six RNase PH subunits, all six RNase PH monomers are catalytically active in the homohexameric RNase PH. Modeling of the Mth exosome RNase PH ring, overview
malfunction
-
absence of RNase PH and polynucleotide phosphorylase, EC 2.7.7.8, causes growth defects. Absence of both enzymes results in the appearance and accumulation of novel mRNA degradation fragments, which are also observed in strains containing mutations in RNase R and PNPase, enzymes whose collective absence is known to cause an accumulation of structured RNA fragments. Single or double deletion of either pnp or rph had a moderate effect on the rpsO, trxA, or lpp mRNAs
malfunction
-
in the absence of RNase PH, there is no 3' end trimming of 16S rRNA and no accumulation of rRNA fragments, and total RNA degradation is greatly reduced. In contrast, the degradation pattern in quality control remains unchanged when RNase PH is absent
malfunction
-
absence of RNase PH and polynucleotide phosphorylase, EC 2.7.7.8, causes growth defects. Absence of both enzymes results in the appearance and accumulation of novel mRNA degradation fragments, which are also observed in strains containing mutations in RNase R and PNPase, enzymes whose collective absence is known to cause an accumulation of structured RNA fragments. Single or double deletion of either pnp or rph had a moderate effect on the rpsO, trxA, or lpp mRNAs
-
malfunction
-
in the absence of RNase PH, there is no 3' end trimming of 16S rRNA and no accumulation of rRNA fragments, and total RNA degradation is greatly reduced. In contrast, the degradation pattern in quality control remains unchanged when RNase PH is absent
-
metabolism
-
RNase PH is involved in the starvation rRNA degradative pathway
metabolism
-
RNase PH is involved in the starvation rRNA degradative pathway
-
physiological function
-
role for RNase PH in the degradation of structured RNA, overview
physiological function
-
the enzym eis required for the pathway of ribosomal RNA degradation during glucose starvation, not for the pathway of ribosomal RNA degradation in quality control during steady-state growth
physiological function
during ribosome degradation in starving cells, RNase II regulates the amount of RNase PH present, via RNase PH stability. RNase PH normally decreases as much as 90% during starvation, in the absence of RNase II the amount of RNase PH remains relatively unchanged. In the presence of RNase II, nutrient deprivation leads to a dramatic reduction in the amount of RNase PH, thereby limiting the extent of rRNA degradation and ensuring cell survival. In the absence of RNase II, RNase PH levels remain high, leading to excessive ribosome loss and ultimately to cell death
physiological function
laboratory strains MG1655 and W3110 have naturally acquired the Rph-1 allele, encoding a truncated catalytically inactive RNase PH protein. Rph-1 protein inhibits RNase P-mediated 5'-end maturation of primary pre-tRNAs with leaders of less than 5 nucleotides in the absence of RppH, an RNA diphosphohydrolase. RppH is not required for 5'-end maturation of endonucleolytically generated pre-tRNAs in the Rph-1 strain and for any tRNAs in Rph mutant or Rp+x03 strains
physiological function
polynucleotide phosphorylase and RNase PH interact to support sRNA stability, activity, and base pairing in exponential and stationary growth conditions. They facilitate the stability and regulatory function of the sRNAs RyhB, CyaR, and MicA during exponential growth. Polynucleotide phosphorylase may contribute to pairing between RyhB and its mRNA targets. During stationary growth, each sRNA responds differently to the absence or presence of PNPase and RNase PH. Polynucleotide phosphorylase and RNase PH stabilize only Hfq-bound sRNAs
physiological function
-
role for RNase PH in the degradation of structured RNA, overview
-
physiological function
-
the enzym eis required for the pathway of ribosomal RNA degradation during glucose starvation, not for the pathway of ribosomal RNA degradation in quality control during steady-state growth
-
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Cudny, H.; Deutscher, M.P.
3 Processing of tRNA precursors in ribonuclease-deficient Escherichia coli. Development and characterization of an in vitro processing system and evidence for a phosphate requirement
J. Biol. Chem.
263
1518-1523
1988
Escherichia coli
brenda
Deutscher, M.P.; Marshall, G.T.; Cudney, H.
RNase PH: an Escherichia coli phosphate-dependent nuclease distinct from polynucleotide phosphorylase
Proc. Natl. Acad. Sci. USA
85
4710-4714
1988
Escherichia coli
brenda
Jensen, K.F.; Andersen, J.T.; Poulsen, P.
Overexpression and rapid purification of the orfE/rph gene product, RNase PH of Escherichia coli
J. Biol. Chem.
267
17147-17152
1992
Escherichia coli
brenda
Kelly, K.O.; Deutscher, M.P.
Characterization of Escherichia coli RNase PH
J. Biol. Chem.
267
17153-17158
1992
Escherichia coli
brenda
Ost, K.A.; Deutscher, M.P.
RNase PH catalyzes a synthetic reaction, the addition of nucleotides to the 3 end of RNA
Biochimie
72
813-818
1990
Escherichia coli
brenda
Zhou, Z.; Deutscher, M.P.
An essential function for the phosphate-dependent exoribonucleases RNase PH and polynucleotide phosphorylase
J. Bacteriol.
179
4391-4395
1997
Escherichia coli
brenda
Symmons, M.F.; Williams, M.G.; Luisi, B.F.; Jones, G.H.; Carpousis, A.J.
Running rings around RNA: a superfamily of phosphate-dependent RNases
Trends Biochem. Sci.
27
11-18
2002
Saccharomyces cerevisiae, Escherichia coli, Streptomyces coelicolor
brenda
Choi, J.M.; Park, E.Y.; Kim, J.H.; Chang, S.K.; Cho, Y.
Probing the functional importance of the hexameric ring structure of RNase PH
J. Biol. Chem.
279
755-764
2004
Pseudomonas aeruginosa
brenda
Wen, T.; Oussenko, I.A.; Pellegrini, O.; Bechhofer, D.H.; Condon, C.
Ribonuclease PH plays a major role in the exonucleolytic maturation of CCA-containing tRNA precursors in Bacillus subtilis
Nucleic Acids Res.
33
3636-3643
2005
Bacillus subtilis
brenda
Harlow, L.S.; Kadziola, A.; Jensen, K.F.; Larsen, S.
Crystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis and implications for its quaternary structure and tRNA binding
Protein Sci.
13
668-677
2004
Bacillus subtilis
brenda
Bralley, P.; Gust, B.; Chang, S.; Chater, K.F.; Jones, G.H.
RNA 3-tail synthesis in Streptomyces: in vitro and in vivo activities of RNase PH, the SCO3896 gene product and polynucleotide phosphorylase
Microbiology
152
627-636
2006
Streptomyces coelicolor, Streptomyces coelicolor M145
brenda
Anderson, J.R.; Mukherjee, D.; Muthukumaraswamy, K.; Moraes, K.C.; Wilusz, C.J.; Wilusz, J.
Sequence-specific RNA binding mediated by the RNase PH domain of components of the exosome
RNA
12
1810-1816
2006
Homo sapiens
brenda
von Braun, S.S.; Sabetti, A.; Hanic-Joyce, P.J.; Gu, J.; Schleiff, E.; Joyce, P.B.
Dual targeting of the tRNA nucleotidyltransferase in plants: not just the signal
J. Exp. Bot.
58
4083-4093
2007
Arabidopsis thaliana
brenda
Ng, C.L.; Waterman, D.G.; Antson, A.A.; Ortiz-Lombardia, M.
Structure of the Methanothermobacter thermautotrophicus exosome RNase PH ring
Acta Crystallogr. Sect. D
66
522-528
2010
Methanothermobacter thermautotrophicus
brenda
Jain, C.
Novel role for RNase PH in the degradation of structured RNA
J. Bacteriol.
194
3883-3890
2012
Escherichia coli, Escherichia coli MG1655
brenda
Basturea, G.N.; Zundel, M.A.; Deutscher, M.P.
Degradation of ribosomal RNA during starvation: comparison to quality control during steady-state growth and a role for RNase PH
RNA
17
338-345
2011
Escherichia coli, Escherichia coli MG1655
brenda
Cameron, T.A.; De Lay, N.R.
The phosphorolytic exoribonucleases polynucleotide phosphorylase and RNase PH stabilize sRNAs and facilitate regulation of their mRNA targets
J. Bacteriol.
198
3309-3317
2016
Escherichia coli (P0CG19), Escherichia coli
brenda
Bowden, K.; Wiese, N.; Perwez, T.; Mohanty, B.; Kushner, S.
The rph-1-encoded truncated RNase PH protein inhibits RNase P maturation of pre-tRNAs with short leader sequences in the absence of RppH
J. Bacteriol.
199
e00301
2017
Escherichia coli (P0CG19), Escherichia coli
brenda
Sulthana, S.; Quesada, E.; Deutscher, M.P.
RNase II regulates RNase PH and is essential for cell survival during starvation and stationary phase
RNA
23
1456-1464
2017
Escherichia coli (P0CG19), Escherichia coli
brenda