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Information on EC 2.7.7.56 - tRNA nucleotidyltransferase
for references in articles please use BRENDA:EC2.7.7.56
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.7 Nucleotidyltransferases
2.7.7.56 tRNA nucleotidyltransferase
IUBMB Comments
Brings about the final exonucleolytic trimming of the 3′-terminus of tRNA precursors in Escherichia coli by a phosphorolysis, producing a mature 3′-terminus on tRNA and nucleoside diphosphate. Not identical with EC 2.7.7.8 polyribonucleotide nucleotidyltransferase.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 2.7.7.56
- polynucleotide
- exoribonuclease
- pnpases
-
exosome
-
phosphorolytic
-
cca-adding
- aminoacylation
-
exonucleolytic
- 3'-terminus
-
2.7.7.25
-
pyre
- trnaphe
showSynonyms
trna nucleotidyltransferase, rnase ph, rph-1, ribonuclease ph, rnase ph ring, phosphate-dependent exonuclease, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
nuclease, ribo-, PH
-
-
-
-
phosphate-dependent exonuclease
-
-
-
-
ribonuclease PH
-
-
-
-
RNase PH
RNase PH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
tRNAn+1 + phosphate = tRNAn + a nucleoside diphosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
tRNA processing
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SYSTEMATIC NAME
IUBMB Comments
tRNA:phosphate nucleotidyltransferase
Brings about the final exonucleolytic trimming of the 3'-terminus of tRNA precursors in Escherichia coli by a phosphorolysis, producing a mature 3'-terminus on tRNA and nucleoside diphosphate. Not identical with EC 2.7.7.8 polyribonucleotide nucleotidyltransferase.
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CAS REGISTRY NUMBER
COMMENTARY
116412-36-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
poly(A) + phosphate
?
-
Substrates: phosphorolysis of poly(A) 15times more rapidly than of tRNA-C-C-A-Cn
Products: -
Products: -
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: -
Products: -
Products: -
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: substrate specificity
Products: -
Products: -
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: dependent on phosphate
Products: -
Products: -
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: dependent on phosphate
Products: enzyme can utilize all dinucleotides as substrates for the reverse reaction
Products: enzyme can utilize all dinucleotides as substrates for the reverse reaction
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: phosphorolysis of poly(A) 15times more rapidly than of tRNA-C-C-A-Cn
Products: -
Products: -
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: tRNA-C-C-A-Cn
Products: -
Products: -
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: reverse reaction is synthetic
Products: -
Products: -
ir
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: 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
Products: -
Products: -
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: implicated in the 3'-processing of tRNA precursors
Products: -
Products: -
ir
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: implicated in the 3'-processing of tRNA precursors
Products: -
Products: -
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: role in tRNA processing and RNA degradation
Products: -
Products: -
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: -
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: implicated in the 3'-processing of tRNA precursors
Products: -
Products: -
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: -
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: plays a major role in the exonucleolytic maturation of CCA-containing tRNA precursors, degradation of the last few nucleotides before the acceptor stem
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: involved in the maturation of tRNA precursors and especially important for removal of nucleotide residues near the CCA acceptor end of the mature tRNAs
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: -
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: the enzyme is a 3' to 5' RNase. The enzyme digests through RNA duplexes of moderate stability
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: degradation of 16S rRNA substrate 3' end
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: the enzyme is a 3' to 5' RNase. RNase PH uses phosphate as a nucleophile to catalyze RNA cleavage
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: 16S rRNA substrate
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: the enzyme is a 3' to 5' RNase. The enzyme digests through RNA duplexes of moderate stability
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: the enzyme is a 3' to 5' RNase. RNase PH uses phosphate as a nucleophile to catalyze RNA cleavage
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: degradation of 16S rRNA substrate 3' end
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: 16S rRNA substrate
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: -
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: 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
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: -
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the reaction proceeds via strongly bound phosphate ions in the phosphorolytic active sites of mthRrp41 protein
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: reverse reaction is synthetic
Products: -
Products: -
ir
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: 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
Products: -
Products: -
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: implicated in the 3'-processing of tRNA precursors
Products: -
Products: -
ir
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: implicated in the 3'-processing of tRNA precursors
Products: -
Products: -
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: role in tRNA processing and RNA degradation
Products: -
Products: -
r
tRNAn+1 + phosphate
tRNA + a nucleoside diphosphate
-
Substrates: implicated in the 3'-processing of tRNA precursors
Products: -
Products: -
r
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: plays a major role in the exonucleolytic maturation of CCA-containing tRNA precursors, degradation of the last few nucleotides before the acceptor stem
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: involved in the maturation of tRNA precursors and especially important for removal of nucleotide residues near the CCA acceptor end of the mature tRNAs
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: the enzyme is a 3' to 5' RNase. The enzyme digests through RNA duplexes of moderate stability
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: degradation of 16S rRNA substrate 3' end
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: the enzyme is a 3' to 5' RNase. The enzyme digests through RNA duplexes of moderate stability
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: degradation of 16S rRNA substrate 3' end
Products: -
Products: -
?
tRNAn+1 + phosphate
tRNAn + a nucleoside diphosphate
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
KCl
Mg2+
Mn2+
additional information
Co2+
-
30% of the activity with Mg2+, 2 mM somewhat more effective than 5 mM
Mn2+
-
40% of the activity with Mg2+, 2 mM somewhat more effective than 5 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme appears to be sensitive to the CCA motif and is surprisingly slow to remove the last nucleotide to generate the functional tRNA
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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.
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
full-length protein with translational start at ATG1 (Met1) and two splice variants with translational start at ATG2 (Met6) and ATG3 (Met69)
-
-
brenda
enzyme mutant deficient in tRNA nucleotidyltransferase and polynucleotide phosphorylase activity
-
-
brenda
naturally acquired truncated inactive ribonuclease PH variant
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
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
-
brenda
-
partial localisation of full-length protein and isoform with translational start at ATG2 (Met6), targeting dependent not only on N-terminal 68 amino acids
brenda
-
partial localisation of full-length protein and isoform with translational start at ATG2 (Met6), targeting dependent not only on N-terminal 68 amino acids
brenda
-
localisation of isoform with translational start at ATG3 (Met69), lacking N-terminal 68 residues
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
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
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
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
-
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
-
Show AA Sequence and Transmembrane Helices (12462 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
-
multisubunit RNA processing enzyme including a ring of six RNase PH subunits
additional information
additional information
-
enzyme mutant deficient in tRNA nucleotidyltransferase and polynucleotide phosphorylase activity shows differing ribosome structure, the 50S subunit is reduced, the 23S subunit is degraded
additional information
-
the 1.9 A crystal structures of the apo and the phosphate-bound forms of RNase PH from reveal a monomeric RNase PH with an alpha/beta-fold tightly associated into a hexameric ring structure in the form of a trimer of dimers
additional information
-
structure elements of RNase pH-like proteins
additional information
-
structure elements of RNase pH-like proteins
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method, wild-type and triple mutant R68Q-R73Q-R76Q RNase PH crystallized and the structures determined by X-ray diffraction to medium resolution. Wild-type and triple mutant RNase PH crystallize as a hexamer and dimer, respectively
-
purified recombinant mthRrp41-mthRrp42 protein complex, hanging-drop vapour diffusion, 0.001 ml of protein in 25 mM Tris pH 7.5, 0.15 M NaCl, mixed with 0.001 ml of reservoir solution containing 5% 2-propanol, 20% PEG 3350, and 0.1 M succinic acid pH 7.0, X-ray diffraction structure determination and analysis at 2.65 A resolution
-
hanging-drop vapor diffusion method. The 1.9 A crystal structures of the apo and the phosphate-bound forms of RNase PH from reveal a monomeric RNase PH with an alpha/beta-fold tightly associated into a hexameric ring structure in the form of a trimer of dimers
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R68Q-R73Q-R76Q
-
triple mutant RNase PH crystallize as a dimer, compared to wild-type enzyme that crystallizes as a hexamer
R69S/R77S
-
mutation leads to the dissociation of RNase PH hexamer into dimers without perturbing the overall monomeric structure
R74S
-
mutation leads to the dissociation of RNase PH hexamer into dimers without perturbing the overall monomeric structure
R74S/R77S
-
mutation leads to the dissociation of RNase PH hexamer into dimers without perturbing the overall monomeric structure
additional information
-
enzyme mutant deficient in tRNA nucleotidyltransferase and polynucleotide phosphorylase activity grows slowly at 37°C, shows a dramatically reduced tRNATyrsu3+ suppressor activity, displays reversible cold-sensitivity, and performs normal tRNA synthesis, ribosome structure and function are severely affected, particularly at lower temperatures of 31°C and below
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
additional information
-
enzyme mutant deficient in tRNA nucleotidyltransferase and polynucleotide phosphorylase activity displays reversible cold-sensitivity, ribosome structure and function are severely affected, particularly at lower temperatures of 31°C and below
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged mthRrp41-mthRrp42 protein complex from Escherichi coli strain E2566 by nickel affinity chromatography and ultrafiltration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
from total RNA into pBluescript II KS+ for sequencing, in pAS2 for subcloning, in pBIN35S35SEmGFP for transformation of tobacco protoplasts and expression as GFP fusion protein, in p426 for generation of three isoforms with alternative ATG start codons ATG1 (Met1), ATG2 (Met6), ATG3 (Met69)
-
genes mth682 and mth683 encode the mthRrp41-mthRrp42 protein complex, cloning and recombinant expression of the His-tagged protein complex in Escherichia coli strain E2566
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Escherichia coli, Saccharomyces cerevisiae, 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
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