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
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e-mediated
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e-like
- 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
- 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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Substrates Products
Substrates Products on EC 3.1.26.12 - ribonuclease E
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REACTION DIAGRAM
13mer nucleotide sequence of RNAI + H2O
?
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endonucleolytic cleavage, a synthetic 13-nt oligoribonucleotide, representing the cleavage site of RNAI, from the 5' end, with the canonical RNase E cleavage site located between U5 and A6
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?
5' monophosphorylated RNA oligonucleotides + H2O
?
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several synthetic substrates, overview
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?
5'-capped RNA I.26 + H2O
?
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low activity, cleavage of the 5' substrate end
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-
?
5'-GAGACAGUAUUUG + H2O
5'-GAGACAGU + AUUUG
LU13 substrate, LU13 is a BR13 derivative that has the central G of the 5' triplet replaced with an A. 5'-biotinylated LU13 is cleaved more rapidly when conjugated to streptavidin prior to incubation with N-terminal half-RNase E. In the absence of streptavidin conjugation, 5'-biotinylated LU13 is cleaved as poorly as its 5' hydroxylated equivalent
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-
?
5'-GGGACAGUAUUUG + H2O
5'-GGGACAGU + AUUUG
BR13 substrate, RNase E can cleave certain RNAs rapidly without requiring a 5'-monophosphorylated end. Cleavage of 5'-hydroxylated oligonucleotide substrate by the N-terminal half of RNase E. RNase E can bind with higher affinity to a 5'-hydroxylated substrate with multiple single-stranded regions than to a 5'-monophosphorylated substrate with one single-stranded site
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?
5'-labeled RNA oligonucleotides + H2O
?
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synthetic RNA substrate variants based on known enzyme RNA substrate sequences, recombinant Rne498 catalytic domain, cleavage site specificity, overview
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?
5'-triphosphorylated cspA mRNA + H2O
?
RNase E recognizes multiple single-stranded regions in cspA mRNA
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?
5'-triphosphorylated epd-pgk RNA + H2O
?
RNase E cleavage of 5'-triphosphorylated epd-pgkRNA is faster than 5'-triphosphorylated 9S RNA and RNAi, but not as fast as the rate of cleavage of 5'-triphosphorylated cspA mRNA
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?
5'ACAGUAUUUG-fluorescein + H2O
5'ACAGU + AUUUG-fluorescein
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5' monophosphorylated, 3' fluorescein-labeled synthetic substrate with protective 2'-O-methyl groups at all positions based on the 5' cleavage site of pBR322 RNA I
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?
5'AUCAAAGAAA + H2O
5'AUCAAAGA + AA
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5'-labeled synthetic RNA substrate, modified 9S RNA sequence, recombinant Rne498 catalytic domain, no activity with the wild-type 9S RNA sequence 5'AUCAAAUAAA and with modified sequence 5'AUCAGAUAAA
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?
5'AUCAAGUAAA + H2O
5'AUCAAGU + AAA
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low activity, 5'-labeled synthetic RNA substrate, modified 9S RNA sequence, recombinant Rne498 catalytic domain, no activity with the wild-type 9S RNA sequence 5'AUCAAAUAAA and with modified sequence 5'AUCAGAUAAA
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?
5'AUCGAAUAAA + H2O
5'AUCGA + AUAAA
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5'-labeled synthetic RNA substrate, modified 9S RNA sequence, recombinant Rne498 catalytic domain, no activity with the wild-type 9S RNA sequence 5'AUCAAAUAAA and with modified sequence 5'AUCAGAUAAA
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?
5'GGGA(D-dT)CAGUAUUU-fluorescein + H2O
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5' monophosphorylated, 3' fluorescein-labeled synthetic substrate with protective 2'-O-methyl groups at all positions based on the 5' cleavage site of RNA I
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?
Bacillus subtilis aprE leader-lacZ mRNA + H2O
?
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wild-type and mutant substrate, the latter with an exchange of a G and an A at +31 and +32, respectively, cleavage of the Bacillus subtilis transcript in a structure-dependent manner at the 5' end to the U residue at +12 within a double-stranded segment of an AU-rich sequence, which is part of the stem-loop structure at the 5' end of the transcript
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?
bacteriophage T4 gene 32 mRNA + H2O
?
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processing at the -71 site, which forms a stem-loop essential for enzyme activity of RNase E, the putative consensus sequence is RAUUW, mutational disruption of the stem-loop leads to loss of activity, mechanism, overview
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?
BR13N RNA + H2O
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synthetic RNA substrate, the cleavage site is GGGACAGUCUGUG
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?
endonulceolytic cleavage of sodB mRNA
?
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the enzyme cleaves within the sodB 5'-untranslated region in vitro, thereby removing the 5' stem-loop structure that facilitates Hfq and ribosome binding, RNase E cleavage can also occur at a cryptic site that becomes available upon sodB 5'-UTR/RyhB base pairing
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?
fluorogenic oligonucleotides + H2O
?
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5' monophosphorylated or 5' hydroxylated substrates, P-BR14-FD or OH-BR14-FD
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?
MicX + H2O
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endonucleolytic cleavage, wild-type substrate, RNase E-dependent processing stabilizes MicX, a Vibrio cholerae sRNA
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?
MicX_DELTA196-263 mutant + H2O
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endonucleolytic cleavage, a truncated Vibrio cholerae sRNA
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?
oligonucleotide + H2O
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preference for decay intermediates whose 5' end is monophosphorylated. The enzyme can tolerate any unpaired nucleotide (A, G, C, or U) at either of the first two positions, with only modest biases. The optimal spacing between the 5' end and the scissile phosphate is eight nucleotides. 5'-Monophosphate-assisted cleavage also occurs, albeit more slowly, when that spacing is greater or at most one nucleotide shorter than the optimum
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?
pppRNA I.26 + H2O
?
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low activity, cleavage of the 5' substrate end
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?
pRNA I.26 + H2O
?
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a monophosphate at the 5' end of the RNA I substrate stimulates the enzyme 25-30fold, cleavage of the 5' substrate end
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?
Rep mRNA + H2O
?
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the arginine-rich RNA binding domain and the protein scaffold domain of RNase E are dispensable for degradation of the replication initiator protein (Rep) mRNA of the ColE2 plasmid
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?
rne mRNA + H2O
?
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the enzyme autoregulates its expression by cleavage and processing of its own rne mRNA
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?
S20 mRNA + H2O
?
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mRNA encoding ribosomal proteins, a single cleavage site at residues 300/301 is preceded by variable 5' extensions
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?
S20 mRNA t175D + H2O
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ribosomal protein encoding RNA, structure mapping, secondary structure modeling, overview
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?
S20 mRNA t194D + H2O
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ribosomal protein encoding RNA, structure mapping, secondary structure modeling, overview
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?
S20 mRNA t84D + H2O
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ribosomal protein encoding RNA, contains a 5' stem loop with three noncanonical A-G pairs, structure mapping, secondary structure modeling, overview
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?
sodB mRNA + H2O
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RNase E and RNase III are required for sodB RNA decay in vivo
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?
sodB192 mRNA + H2O
?
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cleavage of the 5'-untranslated region in vitro thereby removing the stem loop structure that facilitates Hfq and ribosome binding, additional cleavage at a cryptic site, that becomes available upon sodB5'-UTR/RyhB base pairing, RyhB is a small regulatory RNA involved in sodB translation control, overview
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?
tRNA precursors + H2O
?
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the enzyme, cuts intercistronic regions of putative tRNA precursors, overview
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?
tRNATyrsu3+ + H2O
tRNATyrsu3+ + ?
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a construct of 404 nucleotides containing a leader sequence and the amber suppressor form of tRNATyr
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?
UAUUU-containing RNA oligonucleotide + H2O
?
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G378 mutant substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
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?
UUUUU-containing RNA oligonucleotide + H2O
?
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G378/A379 mutant substrate, p23 RNA variant derived from linearized DraI DN1 or DN34 plasmids, in vitro substrate synthesis by SP6 RNA poylmerase
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?
16s rRNA + H2O
?
RNase E completely suppresses the accumulation of the 16.5S RNA intermediate in the Escherichia coli rne-1 strain
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?
5.8S-like rRNA + ?
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5'-end processing, removal of an internal, transcribed spacer consisting of helices 9 and 10, RNase E is responsible for helix 10 processing, while helix 9 is excised by RNase III
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?
23S rRNA + H2O
5.8S-like rRNA + ?
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5'-end processing, removal of an internal, transcribed spacer consisting of helices 9 and 10, RNase E is responsible for helix 10 processing, while helix 9 is excised by RNase III
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?
23S rRNA + H2O
5.8S-like rRNA + ?
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5'-end processing, removal of an internal, transcribed spacer consisting of helices 9 and 10, RNase E is responsible for helix 10 processing, while helix 9 is excised by RNase III
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?
?
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RNase E is involved in 5'-end 23S rRNA processing, schematic overview, removal of an internal, transcribed spacer consisting of helices 9 and 10, RNase E is responsible for helix 10 processing, while helix 9 is excised by RNase III
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?
23S rRNA + H2O
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RNase E is involved in 5'-end 23S rRNA processing, schematic overview, removal of an internal, transcribed spacer consisting of helices 9 and 10, RNase E is responsible for helix 10 processing, while helix 9 is excised by RNase III
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?
23S rRNA + H2O
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RNase E is involved in 5'-end 23S rRNA processing, schematic overview, removal of an internal, transcribed spacer consisting of helices 9 and 10, RNase E is responsible for helix 10 processing, while helix 9 is excised by RNase III
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?
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host factor required-dependent RNase E cleavage of NifA mRNA is essential for NifA translation. Cleavage site is located at 32 nucleotides upstream of the NifA translational start codon
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?
82 nt of the NifA mRNA + H2O
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host factor required-dependent RNase E cleavage of NifA mRNA is essential for NifA translation. Cleavage site is located at 32 nucleotides upstream of the NifA translational start codon
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?
9S rRNA precursor + H2O
5S rRNA + ?
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very low activity with a covalently closed circular variant of the substrate compared to the linear one, overview
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?
9S rRNA precursor + H2O
5S rRNA + ?
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very low activity with a covalently closed circular variant of the substrate compared to the linear one, overview
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?
9SA RNA + H2O
?
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9Sa is a fragment of the 9S precursor of 5S rRNA
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?
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G378 mutant substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
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?
AAUUU-containing RNA oligonucleotide + H2O
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G378 mutant substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
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?
?
endonucleolytic cleavage, BR13 is an oligoribonucleotide that contains the RNase E-cleaved sequence of RNA I
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?
BR13 + H2O
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i.e. an oligonucleotide that contains the RNase E target site of RNA I. The N-terminal part of the enzyme from Vibrio vulnificus shows the cleavage specificity and activity of the enzyme from Escherichia coli
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?
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i.e. 5'GGGACAGUAUUUG3', 3' fluorescein-labeled substrate
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?
BR13 RNA + H2O
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synthetic RNA substrate, the cleavage site is GGGACAGUAUUUG
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?
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endonucleolytic cleavage, a synthetic 30-mer oligoribonucleotide substrate containing 2'-O-methylated nucleotides at positions 16 and 17
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?
BR30M + H2O
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endonucleolytic cleavage, a synthetic 30-mer oligoribonucleotide substrate containing 2'-O-methylated nucleotides at positions 16 and 17
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?
?
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G378 mutant substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
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?
CAUUU-containing RNA oligonucleotide + H2O
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G378 mutant substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
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?
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degradation of the cspA mRNA in vivo is very rapid at temperatures greater than 30°C, overview
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?
cspA mRNA + H2O
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cleavage at a single site in vitro between two stem-loops about 24 residues 3' to the termination codon and about 31 residues from the 3' end. The site of cleavage is independent of the temperature and largely independent of the phosphorylation status of the 5' end of cspA mRNA, overview
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?
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wild-type substrate, best substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
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?
GAUUU-containing RNA oligonucleotide + H2O
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wild-type substrate, best substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
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?
?
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A379 mutant substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
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?
GUUUU-containing RNA oligonucleotide + H2O
?
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A379 mutant substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
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?
mature 16S rRNA
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RNase G, i.e. CafA protein, and RNase E are both required for the 5' maturation of 16S ribosomal RNA
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?
immature 16S rRNA + H2O
mature 16S rRNA
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secondary processing for formation of the mature 5' terminus
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?
ompA mRNA + H2O
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ompA at a site which is rate determining for degradation and also cleaved by RNase K
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?
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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
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proK primary transcript + H2O
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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
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?
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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
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?
proL primary transcript + H2O
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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
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?
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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
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?
proM primary transcript + H2O
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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
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?
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endonucleolytic cleavage, the precursor of the Escherichia coli tRNATyrSu3, cleavage upstream of the RNase P cleavage site in vitro and in vivo
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pSu3 + H2O
?
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endonucleolytic cleavage, the precursor of the Escherichia coli tRNATyrSu3, cleavage upstream of the RNase P cleavage site in vitro and in vivo, cleavage site mapping, overview, very low activity with the substrate mutants K546A and K552A, lack of Mg2+ leads to unspecific cleavage of pSu3 RNA to small oligoribonucleotides
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?
puf mRNA + H2O
?
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initiation of degradation of the 5' pufQ mRNA segment, expressed from plasmids pBPT8 or pBRMOD11 using the bla promoter of plasmid pBR322, the enzyme discriminates between the two sequences GGCUUU and GAUUUU preferring AU-rich sequences
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?
puf mRNA + H2O
?
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initiation of degradation of the 5' pufQ mRNA segment, expressed from plasmids pBPT8 or pBRMOD11 using the bla promoter of plasmid pBR322, the enzyme discriminates between the two sequences GGCUUU and GAUUUU preferring AU-rich sequences
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?
puf mRNA + H2O
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initiation of degradation of the pufLMX segment, the enzyme does not discriminate between the two sequences GGCUUU and GAUUUU
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?
?
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the enzyme is required for RNA processing and degradation
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RNA + H2O
?
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cleavage site specificity is not affected by temperature, selective cleavage at the 5' end of internucleotide bonds in 3' to 5' direction, cleavage pattern, overview
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?
RNA + H2O
?
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endonucleolytic cleavage, the Arabidopsis enzyme uses single-stranded oligoribonucleotide and chloroplast RNA as substrates, and depends on the number of phosphates at the 5' end, is inhibited by structured RNA, and preferentially cleaves A/U-rich sequences, catalytic domain structure, overview
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?
RNA + H2O
?
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?
RNA + H2O
?
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the enzyme or its isolated N-terminal catalytic domain cleave poly(A) tails on the 3' end of RNA substrates, the RNA degradosome cleaves 3' poly(A) tails of RNA irrespective of the 5' phosphorylation status, while the purified RNase E shows high preference for 5'-monophosphorylated RNA substrates, and low activity with 5'-triphosphate RNA, N-terminal ribonucleolytic domain RTD-RNase E is the catalytic domain and sufficient for activity
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?
RNA + H2O
?
RNase E recognizes RNA secondary structure. Signature on the substrate 50 end recognizes and activates RNase E
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?
RNA + H2O
?
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the enzyme or its isolated N-terminal catalytic domain cleave poly(A) tails on the 3' end of RNA substrates, the RNA degradosome cleaves 3' poly(A) tails of RNA irrespective of the 5' phosphorylation status, while the purified RNase E shows high preference for 5'-monophosphorylated RNA substrates, and low activity with 5'-triphosphate RNA, N-terminal ribonucleolytic domain RTD-RNase E is the catalytic domain and sufficient for activity
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?
RNA + H2O
?
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the enzyme plays a key role in processing and degradation of RNA in Escherichia coli
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?
RNA + H2O
?
RNase E recognizes RNA secondary structure. Signature on the substrate 50 end recognizes and activates RNase E
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RNA + H2O
?
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Mg2+ targets the mgtA transcript which encodes a Mg2+ transporter, for degradation by RNase E
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?
RNA + H2O
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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
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?
RNA + H2O
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RNase E cleaves numerous transcripts at preferred sites by sensing uridine as a 2-nt ruler
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?
RNA I + H2O
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full-length RNA I by plasmids pBR322 or pACY184, cleavage site specificity, overview
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?
RNA I + H2O
?
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the arginine-rich RNA binding domain of RNase E and the protein scaffold domain of RNase E is important for successive exoribonucleolytic degradation of RNAI, suggesting involvement of RhlB. RNase E-PNPase complex formation is not essential for RNAI degradation
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?
RNA I + H2O
?
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full-length RNA I and GGGRNA I encoded by plasmids pBR322, pCML103, or pCML108, RNA binding domain structure, secondary structure of the substrate RNA, complex formation and mechanism, multiple cleavage sites, overview
several fragments, product mapping, overview
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?
?
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5' mono- or triphosphorylated, or 5' hydroxylated substrate
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?
rpsT mRNA + H2O
?
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the substrate encodes the ribosomal protein S20, very low activity with a covalently closed circular variant of the substrate compared to the linear one, overview
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?
rpsT mRNA + H2O
?
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the substrate encodes the ribosomal protein S20
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rpsT mRNA + H2O
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the substrate encodes the ribosomal protein S20, very low activity with a covalently closed circular variant of the substrate compared to the linear one, overview
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?
?
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RhlB is an ATP-dependent motor that unfolds structured RNA for destruction by partner ribonucleases, RhlB associates with the essential endoribonuclease RNase E as part of the multi-enzyme RNA degradosome assembly, RNase E activates RhlB severalfold, determination and analysis of the specific protein interaction sites using limited protease digestion, domain cross-linking and homology modelling. The stoichiometry for RhlB-CTD/RNase E, residues 628-843, complex is 1:1, overview
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?
single-stranded RNA + H2O
?
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RNA substrate specificity of full-length and truncated RNase E in complex with RhlB, overview
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?
single-stranded RNA + H2O
?
preferentially cleaves single-stranded RNAs within U-rich regions. Most cleavage sites contained one or two U. It cleaves the phosphodiester linkage on the 3'-side and generates 5'-phosphate- and 3'-hydroxyl-terminated oligonucleotides. The enzyme cleaves these substrates only in close proximity to the 5'- or 3'-ends suggesting that it requires the presence of a free RNA end. Oligoribonucleotides as short as 10 nt can serve as SSO1404 substrates. Tyr-9, Asp-10, Arg-17, Arg-19, Arg-31, and Phe-37 are important for enzymatic activity. Asp-10 might be the principal catalytic residue. No cleavage of dsRNA substrates prepared by annealing ssRNA substrates. No nuclease activity against either of the DNA substrates. The 39 nucleotide ssRNA substrate AAAUACG-/-U-/-U-/-UUCUCCAUUGUCAUAUUGCGCAUAAGUUGA shows the highest activity among the ssRNA substrates tested
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?
single-stranded RNA + H2O
?
preferentially cleaves single-stranded RNAs within U-rich regions. Most cleavage sites contained one or two U. It cleaves the phosphodiester linkage on the 3'-side and generates 5'-phosphate- and 3'-hydroxyl-terminated oligonucleotides. The enzyme cleaves these substrates only in close proximity to the 5'- or 3'-ends suggesting that it requires the presence of a free RNA end. Oligoribonucleotides as short as 10 nt can serve as SSO1404 substrates. Tyr-9, Asp-10, Arg-17, Arg-19, Arg-31, and Phe-37 are important for enzymatic activity. Asp-10 might be the principal catalytic residue. No cleavage of dsRNA substrates prepared by annealing ssRNA substrates. No nuclease activity against either of the DNA substrates. The 39 nucleotide ssRNA substrate AAAUACG-/-U-/-U-/-UUCUCCAUUGUCAUAUUGCGCAUAAGUUGA shows the highest activity among the ssRNA substrates tested
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?
tRNAArg + tRNAHis + tRNALeu + tRNAPro + ?
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polycistronic transcript, maturation, overview
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?
tRNAArgHisLeuPro precursor + H2O
tRNAArg + tRNAHis + tRNALeu + tRNAPro + ?
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polycistronic transcript, maturation
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?
tRNAArgHisLeuPro precursor + H2O
tRNAArg + tRNAHis + tRNALeu + tRNAPro + ?
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polycistronic transcript, maturation, overview
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?
tRNAArgHisLeuPro precursor + H2O
tRNAArg + tRNAHis + tRNALeu + tRNAPro + ?
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polycistronic transcript, maturation
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?
tRNAGly + tRNACys + tRNALeu + ?
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polycistronic transcript, maturation, cleavage downstream of each tRNA, overview
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?
tRNAGlyCysLeu precursor + H2O
tRNAGly + tRNACys + tRNALeu + ?
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polycistronic transcript, maturation, cleavage downstream of each tRNA
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?
tRNAGlyCysLeu precursor + H2O
tRNAGly + tRNACys + tRNALeu + ?
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polycistronic transcript, maturation, cleavage downstream of each tRNA, overview
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?
tRNAGlyCysLeu precursor + H2O
tRNAGly + tRNACys + tRNALeu + ?
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polycistronic transcript, maturation, cleavage downstream of each tRNA
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?
tRNATyr + ?
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maturation, cleavage of the tyrT transcript, containing two tRNATyr1 sequences separated by a 209-nt spacer region plus a downstream mRNA, at three sites in the speacer region, overview
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?
tRNATyr precursor + H2O
tRNATyr + ?
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maturation, cleavage of the tyrT transcript, containing two tRNATyr1 sequences separated by a 209-nt spacer region plus a downstream mRNA, at three sites in the spacer region
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?
?
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cleavage in the 5' leader sequence, the enzyme is involved in regulation of cellular tRNA levels
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?
tRNATyrSu3 precursor + H2O
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cleavage in the 5' leader sequence, cleavage sites and activity using wild-type and deletion mutant substrates, overview
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?
?
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the unc operon encodes the eight subunits of the Escherichia coli F1F0-ATPase, processing of the unc mRNAs by the RNase E, overview, RNase E is essential for uncC processing
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?
unc mRNA + H2O
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the unc operon encodes the eight subunits of the Escherichia coli F1F0-ATPase, processing of the unc mRNAs by the RNase E, overview
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RNase E is a processing enzyme involved in 3' end formation of M1 RNA, and plays a dual role in processing and degradation to achieve tight control of M1 RNA biosynthesis
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upRNA + H2O
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M1 RNA, the gene product of rnpB, is the catalytic subunit of RNase P in Escherichia coli, M1 RNA is transcribed from a proximal promoter as pM1 RNA, a precursor M1 RNA, and then is processed at its 3' end by RNase E, the M1 RNA structural sequence in upRNA is much more vulnerable to the enzyme than the sequence in pM1 RNA, full-length enzyme and N-terminal domain of RNase E, cleavage patterns, overview
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RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region
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additional information
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RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region
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additional information
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the enzyme prefers 5' monophosphorylated RNA substrates compared to nonphosphorylated or 5' triphosphorylated RNA substrates
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additional information
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Aquifex aeolicus RNase E/G is able to selectively cleave internucleotide bonds in the 3'-5' direction, and to cut in intercistronic regions of putative tRNA precursors
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additional information
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the bifunctional enzyme, exhibiting RNase E and RNase G activities, is involved in rRNA processing and maturation of tRNAs, that originated from polycistronic transcripts encoded by the Aquifex aeolicus tufA2 and rRNA operons, overview
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additional information
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site-specific RNase E/G cleavage of RNA using 5'-end-labelled substrates, e.g. L1 RNA, RNAI, and 9S RNA, overview. RNase E/G has a temperature-dependent, endoribonucleolytic activity that is dependent on the 5'-phosphorylation status of RNA. The enzyme site-specifically cleaves oligonucleotides and structured RNAs at locations that are partly overlapping or completely different when compared to the positions of Escherichia coli RNase E and RNase G cleavage sites, RNase E/G shows 3'-5' directionality in cleavage site selection, overview, the cleavage site selection of RNase E/G is temperature-dependent, overview
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additional information
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RNA degradation in the chloroplast occurs via the polyadenylation-assisted degradation pathway, plant RNase E participates in the initial endonucleolytic cleavage of the polyadenylation-stimulated RNA degradation process in the chloroplast, perhaps in collaboration with the two other chloroplast endonucleases, RNase J and CSP41, overview
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additional information
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initiation of tRNA 5' maturation by RNase E is essential for cell viability, the enzyme initiates the processing of polycistronic RNA of several operons, e.g. of glyW cysT leuZ, argX hisR leuT proM, or lysT valT lysW valZ lysY lysZlysQ, as well as of monocistronic transcripts such as pheU, pheV, asnT, asnU, asnV, or asnW, mapping of cleavage sites at the 3' end within tRNA precursors, overview, the enzyme is essential for degradation of many mRNAs, e.g. of rpsO
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additional information
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RNase E is involved in and interacts with functionally and physically polynucleotide phosphorylase, and also with other enzymes implicated in the processing and degradation of RNA, polynuclease phosphorylase, PNPase, degrades the reaction products generated by RNase E
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additional information
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the enzyme autoregulates its expression by cleavage and processing of its own rne mRNA
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additional information
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the enzyme is essential for regulation of mRNA turnover by specific processing and degradation and is involved in regulation of cell homeostasis, growth and development
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additional information
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the enzyme is essential for regulation of mRNA turnover by specific processing and degradation and is involved in regulation of cell homeostasis, growth and development
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additional information
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the enzyme is part of the RNA degradosome, a large multiprotein machine to process and degrade RNA
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additional information
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the enzyme is required for rapid decay and correct hydrolytic processing of RNA
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additional information
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the enzyme is the major endoribonuclease participating in mRNA turnover in Escherichia coli
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additional information
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the enzyme plays an important role in the processing and degradation of bacteriophage T4 and Escherichia coli mRNAs, mutational processing site analysis, overview
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additional information
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the enzyme, especially its catalytic N-terminal domain, is essential for RNA processing and degradation, and for cell growth and feedback regulation of RNase E synthesis
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additional information
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cleavage site recognition mechanism, effect on substrate structure alteration by different treatments on cleavage site recognition, overview
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additional information
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identification of specific sequence determinants that either facilitate or impede the recognition and cleavage of RNA by the enzyme, RNA-enzyme interactions, overview
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additional information
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nucleic acid binding structure, structure-function relationship, overview
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additional information
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nucleic acid binding structure, structure-function relationship, overview
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additional information
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ribonuclease E is a 5'-end-dependent, single-strand-specific endonuclease that initiates the selective decay of mRNA having regulatory function, regulation of mRNA levels in response to environment, the enzyme proceeds in a 5' to 3' direction, the enzyme shows high activity with 5' monophosphorylated RNA, but low activity with 5' triphosphorylated RNA, poor activity with circular RNA substrates, overview
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additional information
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RNA processing reaction mechanism and involved functional groups, activity depends on protonated and unprotonated groups, the recognition of a guanosine sequence determinant upstream of the scissile bond via interaction with the exocyclic 2-amino group, the 7N of the nucleobase, and the imino proton or 6-keto group, overview
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additional information
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RNase E acts via a scanning mechanism in processing and degradation of RNA
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additional information
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RNase E shows preference for 5' monophosphorylated RNA substrates rather than RNA with a triphosphate or hydroxyl at the 5' end, the enzyme needs to be in a multimeric state for activation by 5' monophosphorylated RNA substrates
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additional information
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structural features required for RNA turnover, the enzyme attacks the 5' terminus of RNA substrates, RNA recognition mechanism, RNA-binding channel formed by the catalytic domain tetramer, cleavage site structure, and reaction mechanism, overview
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additional information
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structural features required for RNA turnover, the enzyme attacks the 5' terminus of RNA substrates, RNA recognition mechanism, RNA-binding channel formed by the catalytic domain tetramer, cleavage site structure, and reaction mechanism, overview
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additional information
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the catalytic domain of the multifunctional endoribonuclease determines inherent 3' to 5' directionality in cleavage site selection, cleavage site sequences overview
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additional information
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the enzyme shows similar cleavage site specificity as RNase G
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additional information
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the N-terminal catalytic domain is sufficient for catalytic activity, the enzyme shows high RNA binding ability, and cleavage of mRNA and rRNA, RNase E interacts with polynucleotide phosphorylase and other enzymes implicated in the processing and degradation of RNA, cleavage site specificity, overview, RNase E requires the stem loop structure in RNA substrates, altering of the substrate secondary structure alters substrate specificity, overview, the enzymes' arginine-rich RNA-binding site is not essential for activity but allows the degradosome to move progressively along the transcript during degradation
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additional information
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both RNase E and RNase III control the stability of sodB mRNA upon translational inhibition by the small regulatory RNA RyhB, iron-dependent variations in the steady-state concentration and translatability of sodB mRNA are modulated by the small regulatory RNA RyhB, the RNA chaperone Hfq, and RNase E, decay of sodB mRNA is retarded upon inactivation of RNaseE in vivo, mechanism, modelling, overview
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additional information
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ribonuclease E is an essential hydrolytic endonuclease in Escherichia coli, and it plays a central role in maintaining the balance and composition of the messenger RNA population
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additional information
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ribonuclease E is an essential hydrolytic endonuclease in Escherichia coli, and it plays a central role in maintaining the balance and composition of the messenger RNA population
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additional information
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RNase E is an essential bacterial endoribonuclease involved in the turnover of messenger RNA and the maturation of structured RNA precursors in Escherichia coli, RNA degradation mechanism, overview
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additional information
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RNase E is an essential bacterial endoribonuclease involved in the turnover of messenger RNA and the maturation of structured RNA precursors in Escherichia coli, RNA degradation mechanism, overview
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additional information
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RNase E is an essential endonuclease involved in the regulatory processing and/or degradation of tRNAs, rRNAs, and non-coding small RNAs as well as many mRNAs, the enzyme is regulated by an RNA-binding protein Hfq. RNase is required for induction of the glutamate-dependent acid resistance system in a RpoS-independent manner
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additional information
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RNase E is an essential Escherichia coli endoribonuclease that plays a major role in the decay and processing of a large fraction of RNAs in the cell, overview
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additional information
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RNase E is an essential Escherichia coli endoribonuclease that plays a major role in the decay and processing of a large fraction of RNAs in the cell, overview
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additional information
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RNaseE, as the main component of the RNA degradosome of Escherichia coli, plays an essential role in RNA processing and decay
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additional information
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the balance and composition of the transcript population is affected by RNase E, an essential endoribonuclease that not only turns over RNA but also processes certain key RNA precursors
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additional information
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the balance and composition of the transcript population is affected by RNase E, an essential endoribonuclease that not only turns over RNA but also processes certain key RNA precursors
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additional information
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endonucleolytic cleavage as selective processing via allosteric intermediates of RNA substrates, the catalytic activity is influenced by the 5'-end of the substrate, four subunits of RNase E catalytic domain are organized in an interwoven quaternary structure required for catalytic activity, catalytic site structure, overview
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additional information
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endonucleolytic cleavage as selective processing via allosteric intermediates of RNA substrates, the catalytic activity is influenced by the 5'-end of the substrate, four subunits of RNase E catalytic domain are organized in an interwoven quaternary structure required for catalytic activity, catalytic site structure, overview
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additional information
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the enzyme is active on mRNA and tRNA substrates, overview
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additional information
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a proportion of PNPase is recruited into a multi-enzyme assembly, known as the RNA degradosome, through an interaction with the scaffolding domain of the endoribonuclease RNase E
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additional information
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RNase E autoregulates its production by governing the decay rate of RNase E mRNA by binding directly to a stem-loop in the rne gene 5' untranslated region
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additional information
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RNase E preferres substrates possessing a 5'-monophosphate
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additional information
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RNase E preferres substrates possessing a 5'-monophosphate
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additional information
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the C-terminus of this enzyme serves as a scaffold to which other components of the RNA degradosome bind including the phosphorolytic 3'-exonuclease, polynucleotide phosphorylase, the DEAD-box RNA helicase RhlB, and the glycolytic enzyme enolase. The DEAD-box RNA helicases CsdA and RhlE and the RNA binding protein Hfq may bind to RNase E in place of one or more of the prototypical components.
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additional information
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upon catalytic activation, RNase E undergoes a marked conformational change characterized by the coupled movement of two RNA-binding domains to organize the active site
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additional information
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upon catalytic activation, RNase E undergoes a marked conformational change characterized by the coupled movement of two RNA-binding domains to organize the active site
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additional information
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Escherichia coli enolase and its RNase E enolase-binding site demonstrate positive interactions. PNPase-binding site of RNase E interacts with Vibrio angustum S14 or Escherichia coli PNPase
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additional information
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Escherichia coli enolase and its RNase E enolase-binding site demonstrate positive interactions. PNPase-binding site of RNase E interacts with Vibrio angustum S14 or Escherichia coli PNPase
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additional information
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RNase E cleaves the 217-nt RNAs at internal sites in an arginine-rich RNA binding domain-independent manner and about 180-nt degradation intermediates are formed
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additional information
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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 scaffold region of RNase E can be deleted up to residue 750 without losing the ability to cause the rapid degradation of target mRNAs mediated by Hfq/sRNAs. The truncated RNase E750 can still bind to Hfq although the truncation significantly reduces the Hfq-binding ability. Deletion of the 702-50 region greatly impairs the ability of RNase E to cause the degradation of ptsG mRNA. A polypeptide corresponding to the scaffold region binds to Hfq without the help of RNA. Overexpression of RhlB partially inhibits the Hfq binding to RNase E and the rapid degradation of ptsG mRNA
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additional information
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RNase PH interacts with the carboxy-terminal end of RNase E
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additional information
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the enzyme is the major endoribonuclease participating in mRNA turnover in Escherichia coli
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additional information
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the enzyme binds RNA with high affinity
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additional information
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RNase PH interacts with the carboxy-terminal end of RNase E
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additional information
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ribonuclease E is a 5'-end-dependent, single-strand-specific endonuclease that initiates the selective decay of mRNA having regulatory function, regulation of mRNA levels in response to environment, the enzyme proceeds in a 5' to 3' direction, the enzyme shows high activity with 5' monophosphorylated RNA, but low activity with 5' triphosphorylated RNA, poor activity with circular RNA substrates, overview
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additional information
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the C-terminus of this enzyme serves as a scaffold to which other components of the RNA degradosome bind including the phosphorolytic 3'-exonuclease, polynucleotide phosphorylase, the DEAD-box RNA helicase RhlB, and the glycolytic enzyme enolase. The DEAD-box RNA helicases CsdA and RhlE and the RNA binding protein Hfq may bind to RNase E in place of one or more of the prototypical components.
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additional information
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analysis of cleavage site specficity
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additional information
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RNase E plays an essential role in the maturation of tRNA precursors, cleavage site and maturation process modeling, overview
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additional information
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the enzyme can cleave internucleotide bonds in the bubble regions of duplex RNA segments and in single-stranded regions, mechanism
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additional information
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RNase E plays an essential role in the maturation of tRNA precursors, cleavage site and maturation process modeling, overview
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additional information
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the enzyme is active on mRNA and tRNA substrates, overview
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additional information
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RNase E enolase-binding site interacts with enolase from both Vibrio angustum S14 and Escherichia coli. The C-terminal half of RNase E interacts with Vibrio angustum S14 or Escherichia coli PNPase. C-terminal half of RNase E is capable of self-interaction
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additional information
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RNase E enolase-binding site interacts with enolase from both Vibrio angustum S14 and Escherichia coli. The C-terminal half of RNase E interacts with Vibrio angustum S14 or Escherichia coli PNPase. C-terminal half of RNase E is capable of self-interaction
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additional information
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substrate specificity, the enzyme shows high activity with 5' monophosphorylated RNA, but low activity with 5' triphosphorylated RNA, overview
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additional information
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cleavage site specificity, overview
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additional information
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substrate specificity, the enzyme shows high activity with 5' monophosphorylated RNA, but low activity with 5' triphosphorylated RNA, overview
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additional information
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substrate specificity, the enzyme shows high activity with 5' monophosphorylated RNA, but low activity with 5' triphosphorylated RNA, overview
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additional information
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RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region
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additional information
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N-RneV has cleavage activity and specificity of RNase E on RNase E-targeted sequence of RNA I (BR13)
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additional information
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N-RneV has cleavage activity and specificity of RNase E on RNase E-targeted sequence of RNA I (BR13)
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