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
-
autoregulation
-
e-mediated
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e-like
- ompa
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endoribonucleolytic
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5'-terminal
-
intercistronic
-
cole1-type
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monophosphorylated
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5'-monophosphorylated
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shine-dalgarno
-
rho-independent
-
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
3.1.26.12 ribonuclease EAdvanced search results
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results (Inhibitors
Inhibitors on EC 3.1.26.12 - ribonuclease E
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
Diamide
treatment of the N-terminal catalytic domain with diamide causes complete loss of the zinc, but only slightly reduced activity as tetramer
ribosomal protein L4
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L4 interacts with a site outside of the catalytic domain at the C-terminal domain of RNase E to regulate the endoribonucleolytic functions of the enzyme thus inhibiting RNase E-specific cleavage in vitro
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RraB
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in vitro cleavage of p23 RNA by 70 ng RNAse ES is inhibited by 20.3% by RraB
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RraA
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in vitro cleavage of p23 RNA by 70 ng RNAse ES is inhibited by 38.9% by RraA
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RraAV1
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the coexpression of RraAV1 more efficiently inhibits RNase E action than coexpression of RraA
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RraAV1
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inhibits the enzymatic activity of RNase EV in vivo and in vitro by interacting with the C-terminal domain of RNase EV. RraAV1 efficiently inhibits the ribonucleolytic activity of RNase EV on BR10 + hpT, a synthetic oligonucleotide containing the RNase E cleavage site of RNA I
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additional information
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sequences sequestering the -71 site of bacteriophage T4 gene 32 mRNA inhibit the enzyme
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additional information
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anti-sense deoxynucleotide constructs complementary to the 5' end sequences of RNA substrates reduce the enzyme activity
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additional information
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the enzyme is not inhibitable by commercially available RNase A inhibitor
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additional information
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2'-O-methyl nucleotide substitutions in the synthetic RNA substrate, e.g. in RNA BR13-13M, inhibit the enzyme
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additional information
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RraB binds to the C-terminal region of RNase E, thus affecting both the protein composition of the degradosome and the endonucleolytic activity of RNase E. The glmS852::Tn5 allele results in an approximately 50% lower intracellular concentration of uridine 5'-diphospho-N-acetyl-glucosamine and confers a 5fold increase in the level of rraB mRNA, thereby lowering the RNase E activity. Reduction in cellular concentration of uridine 5'-diphospho-N-acetyl-glucosamine by the glmS852::Tn5 allele mediating a 2fold increase in beta-galactosidase activity from a chromosomal fusion of the 5' untranslated region of the rne gene to lacZ, results in increased expression of RraB, which may modulate the action of RNase E
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additional information
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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 E complex loses cleavage activity in the absence of host factor required
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