3.1.26.12: ribonuclease E
This is an abbreviated version!
For detailed information about ribonuclease E, go to the full flat file.
Word Map on EC 3.1.26.12
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3.1.26.12
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degradosome
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polynucleotide
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phosphorylase
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pnpase
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srnas
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endonuclease
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hfq
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helicase
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endonucleolytic
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exoribonuclease
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single-stranded
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enolase
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stem-loops
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polya
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rna-binding
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polycistronic
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ribonucleolytic
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e-dependent
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base-pairing
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dead-box
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autoregulation
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e-mediated
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e-like
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ompa
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endoribonucleolytic
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5'-terminal
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intercistronic
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cole1-type
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monophosphorylated
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5'-monophosphorylated
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shine-dalgarno
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rho-independent
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hfq-dependent
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glucosamine-6-phosphate
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riboswitches
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au-rich
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glm
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rna-processing
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crescentus
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analysis
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medicine
- 3.1.26.12
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degradosome
- polynucleotide
- phosphorylase
- pnpase
- srnas
- endonuclease
- hfq
- helicase
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endonucleolytic
- exoribonuclease
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single-stranded
- enolase
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stem-loops
- polya
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rna-binding
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polycistronic
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ribonucleolytic
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e-dependent
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base-pairing
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dead-box
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autoregulation
-
e-mediated
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e-like
- ompa
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endoribonucleolytic
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5'-terminal
-
intercistronic
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cole1-type
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monophosphorylated
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5'-monophosphorylated
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shine-dalgarno
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rho-independent
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hfq-dependent
- glucosamine-6-phosphate
- riboswitches
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au-rich
- glm
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rna-processing
- crescentus
- analysis
- medicine
Reaction
endonucleolytic cleavage of single-stranded RNA in A- and U-rich regions =
Synonyms
Ams/Rne/Hmp1 polypeptide, AqaRng, endoribonuclease E, endoribonuclease RNase E, More, NCgl2281, ribonuclease E, RNase E, RNase E/G, RNase E/G-type endoribonuclease, RNase ES, RNase EV, RNaseE, Rne, Rne protein, RneC, Rng, SSO1404, SynRne
ECTree
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General Information
General Information on EC 3.1.26.12 - ribonuclease E
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evolution
malfunction
metabolism
physiological function
characterization of the RNase E-PNPase interaction in alpha-proteobacteria, gamma-proteobacteria and cyanobacteria suggests that it arose independently several times during evolution, thus conferring an advantage in control and coordination of RNA processing and degradation
evolution
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characterization of the RNase E-PNPase interaction in alpha-proteobacteria, gamma-proteobacteria and cyanobacteria suggests that it arose independently several times during evolution, thus conferring an advantage in control and coordination of RNA processing and degradation
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RNAI signals of the DELTA225 mutant lacking the PNPase binding region are similar to those of the wild-type strain. RNAI degradation intermediate accumulates in the DELTA374 mutant lacking the PNPase binding region and protein scaffold domain, which binds to RhlB and enolase, as compared with that in the wild-type strain
malfunction
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absence of RNase E differentially affects the decay of specific mRNAs. Neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneD1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the predicted RNase H domain of RNase G, generating the rng-219 and rng-248 alleles, result in complementation of the growth defect associated with various RNase E mutants
malfunction
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an NCgl2281 knockout mutant accumulates 5S rRNA precursor molecules. The processing of 16S and 23S rRNA, tRNA, and tmRNA is normal in the mutant cells. Primer extension analysis reveals that the RNase E/G orthologue cleaves at the -1 site of the 5' end of 5S rRNA. Mapping of the 5' and 3' ends of 5S rRNA precursors in NCgl2281 knockout mutant, overview
malfunction
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mutations in endoribonucleases RNase E reduce Salmonella virulence capacity. Mutants display an impaired motility, by forming a barely detectable motility ring after 8 h of incubation that remains much smaller than the one formed by the wild type after 24 h of incubation
malfunction
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RNase E deletion or inactivation of temperature-sensitive RNase E protein precludes normal initiation of the SOS response. RNase E-deficient cells remain able to produce RNA and protein during the period when SOS response is inhibited by lack of the enzyme
malfunction
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an NCgl2281 knockout mutant accumulates 5S rRNA precursor molecules. The processing of 16S and 23S rRNA, tRNA, and tmRNA is normal in the mutant cells. Primer extension analysis reveals that the RNase E/G orthologue cleaves at the -1 site of the 5' end of 5S rRNA. Mapping of the 5' and 3' ends of 5S rRNA precursors in NCgl2281 knockout mutant, overview
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the endoribonuclease RNase E of Escherichia coli is an essential enzyme that plays a major role in all aspects of RNA metabolism
metabolism
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direct entry by RNase E has a major role in bacterial RNA metabolism. Direct entry is mediated by specific unpaired regions that are adjacent to, but not contiguous with, segments cleaved by RNase E. A 5'-monophosphate is not required to activate the catalytic step
metabolism
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RNase E-dependent degradation of sinI mRNA from the 5'-end is one of the steps mediating a high turnover of sinI mRNA, which allows the Sin quorum-sensing system to respond rapidly to changes in transcriptional control of N-acyl-homoserine lactone production. RNase E acts on the 5'-untranslated region of sinI independently of the posttranscriptional regulator Hfq
metabolism
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RNase E-dependent degradation of sinI mRNA from the 5'-end is one of the steps mediating a high turnover of sinI mRNA, which allows the Sin quorum-sensing system to respond rapidly to changes in transcriptional control of N-acyl-homoserine lactone production. RNase E acts on the 5'-untranslated region of sinI independently of the posttranscriptional regulator Hfq
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RNase E is involved in the post-transcriptional regulation of NifA expression. Host factor required-dependent RNase E cleavage is essential for NifA translation, probably by making ribosome-binding sites accessible
physiological function
RNase E microdomain sequences are well-conserved with those described in Escherichia coli. The RNase E C-terminal half is less conserved and structured than its N-terminal half. RNase E is a hub protein with multiple interaction interfaces that are under different evolutionary pressures. RNase E can rescue the temperature sensitive rne-1 phenotype of Escherichia coli
physiological function
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NCgl2281 endoribonuclease is involved in the 5' maturation of 5S rRNA
physiological function
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RNase E is a key component of the RNA degradosome, a multienzyme complex hat plays a central role in mRNA turnover and the processing of stable RNA in eubacteria. The degradosome is composed of a tetramer of RNase E molecules interacting via their N-terminal regions, with the C-terminal end of each RNase E molecule complexed with a monomer of RhlB, a dimer of enolase, and a trimer of PNPase
physiological function
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RNase E is essential for cell viability and plays a major role in mRNA decay, rRNA maturation, tRNA processing, and a variety of other aspects of RNA metabolism. Maturation of tRNACys, tRNAHis, and tRNAPro but not tRNAAsn is completely dependent on RNase E
physiological function
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RNase E is responsible for the functional interaction with Hfq to cause the sRNA-mediated destabilization of target mRNAs. the RNA chaperon Hfq along with Hfq-binding sRNAs stably binds to RNase E in Escherichia coli. The role of the Hfq-RNase E interaction is to recruit RNase E to target mRNAs of sRNAs resulting in the rapid degradation of the mRNA-sRNA hybrid. The C-terminal scaffold region of RNase E is responsible for the interaction with Hfq. Mutational interaction analysis, overview
physiological function
the phosphate sensor domain in the enzyme is required for efficient autoregulation of RNase E synthesis. Impact of the 5'-sensor on mRNA stability, overview
physiological function
the role in the CRISPR-mediated anti-phage defense might involve degradation of phage or cellular mRNAs
physiological function
both the full-length and the N-terminal part of RNase EV functionally complement Escherichia coli RNase E and their expression consequently supports normal growth of RNase E-depleted Escherichia coli cells. Escherichia coli cells expressing N-RneV show copy numbers of ColE1-type plasmid similar to that of Escherichia coli cells expressing N-Rne
physiological function
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extraordinarily long antisense RNAs of 3.5 and 7 kb protect a set of mRNAs from RNase E degradation that accumulate during phage infection. These antisense RNA-mRNA duplex formations mask single-stranded recognition sites of RNase E, leading to increased stability of the mRNAs. The interactions directly modulate RNA stability and provide an explanation for enhanced transcript abundance of certain mRNAs during phage infection
physiological function
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knockout mutant cells accumulate 5S rRNA precursor molecules. The processing of 16S and 23S rRNA, tRNA, and tmRNA is normal. RNase E/G cleaves at the -1 site of the 5' end of 5S rRNA. 3' maturation is essentially unaffected
physiological function
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neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with RNase E deletion mutants even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the predicted RNase H domain of RNase G, generating the rng-219 and rng-248 alleles, result in complementation of the growth defect associated with various RNase E mutants, suggesting that this region of the two proteins may help distinguish their in vivo biological activities
physiological function
viable mutations affecting the 5'-phosphate sensor of RNase E, including R169Q or T170A, become lethal when combined with deletions removing part of the non-catalytic C-terminal domain of RNase E. The phosphate sensor is required for efficient autoregulation of RNase E synthesis as RNase E R169Q is strongly overexpressed with accumulation of proteolytic fragments. In addition, mutation of the phosphate sensorstabilizes the rpsT P1 mRNA as much as sixfold and slows the maturation of 16S rRNA. The decay of other model mRNAs and the processing of several tRNA precursors are unaffected by mutations in the phosphate sensor
physiological function
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Escherichia coli cells normally require RNase E activity to form colonies
physiological function
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RNase E function is required to mount a normal SOS response
physiological function
Escherichia coli messenger RNAs are rapidly degraded immediately after bacteriophage T4 infection, and the host RNase E contributes to this process
physiological function
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in the degradation pathway of mRNA for Escherichia coli, the initial cleavage of a transcript by RNase E is followed closely by exonucleolytic degradation of the products by PNPase (polynucleotide phosphorylase), RNase II, or RNase R
physiological function
in the degradation pathway of mRNA for Escherichia coli, the initial cleavage of a transcript by RNase E is followed closely by exonucleolytic degradation of the products by PNPase (polynucleotide phosphorylase), RNase II, or RNase R
physiological function
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proline tRNAs are matured at the 3' end primarily by a direct RNase E endonucleolytic cleavage. RNase E is primarily responsible for the endonucleolytic removal of the entire Rho-independent transcription terminator associated with the proK, proL and proM primary transcripts by cleaving immediately downstream of the CCA determinant
physiological function
RNase E carries out the cleavages that initiate the degradation pathways of rRNA in the quality control process and during starvation
physiological function
RNase E endonuclease is the crRNA maturation enzyme in a CRISPR-Cas subtype III-Bv system. Overexpression of RNase E leads to overaccumulation and knock-down to the reduced accumulation of crRNAs in vivo. RNase E is the limiting factor for CRISPR complex formation
physiological function
RNase E is a central ribonuclease of RNA metabolism and post-transcriptional control of gene expression
physiological function
RNase E is involved in the processing and degradation of nearly every transcript in Escherichia coli
physiological function
RNase E is necessary to maintain the normal abundance of phosphoenolpyruvate synthetase (PpsA) in Escherichia coli. PpsA links the TCA cycle with glycolytic pathway for gluconeogenesis by converting pyruvate to phosphoenolpyruvate. RNase E may function to maintain appropriate carbon flux around phosphoenolpyruvate in Escherichia coli
physiological function
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RNase E processing of various precursor RNAs produces many small regulatory RNAs, constituting a major small-RNA biogenesis pathway in bacteria
physiological function
RNaseE is the main component of the RNA degradosome of Escherichia coli, which plays an essential role in RNA processing and decay
physiological function
the enzyme is an essential bacterial endoribonuclease with a central role in processing tRNAs and rRNA, and turning over mRNAs
physiological function
the enzyme is required for S-adenosylmethionine homeostasis in Sinorhizobium meliloti
physiological function
the enzyme participates in most aspects of RNA processing and degradation
physiological function
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the enzyme plays an important role in RNA processing and decay in Escherichia coli
physiological function
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RNase E is involved in the post-transcriptional regulation of NifA expression. Host factor required-dependent RNase E cleavage is essential for NifA translation, probably by making ribosome-binding sites accessible
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physiological function
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the role in the CRISPR-mediated anti-phage defense might involve degradation of phage or cellular mRNAs
-
physiological function
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the enzyme is required for S-adenosylmethionine homeostasis in Sinorhizobium meliloti
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physiological function
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extraordinarily long antisense RNAs of 3.5 and 7 kb protect a set of mRNAs from RNase E degradation that accumulate during phage infection. These antisense RNA-mRNA duplex formations mask single-stranded recognition sites of RNase E, leading to increased stability of the mRNAs. The interactions directly modulate RNA stability and provide an explanation for enhanced transcript abundance of certain mRNAs during phage infection
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physiological function
Escherichia coli K12 PB103
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RNaseE is the main component of the RNA degradosome of Escherichia coli, which plays an essential role in RNA processing and decay
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physiological function
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Escherichia coli cells normally require RNase E activity to form colonies
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physiological function
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the enzyme participates in most aspects of RNA processing and degradation
-
physiological function
-
in the degradation pathway of mRNA for Escherichia coli, the initial cleavage of a transcript by RNase E is followed closely by exonucleolytic degradation of the products by PNPase (polynucleotide phosphorylase), RNase II, or RNase R
-
physiological function
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RNase E is a central ribonuclease of RNA metabolism and post-transcriptional control of gene expression
-
physiological function
-
RNase E is involved in the processing and degradation of nearly every transcript in Escherichia coli
-
physiological function
-
RNase E carries out the cleavages that initiate the degradation pathways of rRNA in the quality control process and during starvation
-
physiological function
-
RNase E is necessary to maintain the normal abundance of phosphoenolpyruvate synthetase (PpsA) in Escherichia coli. PpsA links the TCA cycle with glycolytic pathway for gluconeogenesis by converting pyruvate to phosphoenolpyruvate. RNase E may function to maintain appropriate carbon flux around phosphoenolpyruvate in Escherichia coli
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physiological function
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Escherichia coli messenger RNAs are rapidly degraded immediately after bacteriophage T4 infection, and the host RNase E contributes to this process
-
physiological function
-
proline tRNAs are matured at the 3' end primarily by a direct RNase E endonucleolytic cleavage. RNase E is primarily responsible for the endonucleolytic removal of the entire Rho-independent transcription terminator associated with the proK, proL and proM primary transcripts by cleaving immediately downstream of the CCA determinant
-
physiological function
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NCgl2281 endoribonuclease is involved in the 5' maturation of 5S rRNA
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physiological function
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knockout mutant cells accumulate 5S rRNA precursor molecules. The processing of 16S and 23S rRNA, tRNA, and tmRNA is normal. RNase E/G cleaves at the -1 site of the 5' end of 5S rRNA. 3' maturation is essentially unaffected
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