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Literature summary for 4.6.1.22 extracted from

  • Condon, C.
    What is the role of RNase J in mRNA turnover? (2010), RNA Biol., 7, 316-321.
    View publication on PubMed
Search for more literature for 4.6.1.22

Inhibitors

Inhibitors Comment Organism Structure
additional information the 5'-to-3' exoribonuclease activity of the enzyme is active on 5'-monophosphorylated or 5'-hydroxylated RNA, but is essentially completely inhibited by the triphosphorylated 5' ends of primary transcripts Bacillus subtilis

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ catalytic metal ion Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bacillus subtilis enzyme RNase J1 possesses 5'-to-3' exoribonuclease activity, while enzymes RNase J1 and RNase J2 form a complex that also has endonuclease activity, model for the degradation of the trp leader mRNA bound to TRAP. RNase J1 is the endonuclease cleaving scRNA that is 4 nts shorter on the 3' end ?
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Organism

Organism UniProt Comment Textmining
Bacillus subtilis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme RNase J1 possesses 5'-to-3' exoribonuclease activity, while enzymes RNase J1 and RNase J2 form a complex that also has endonuclease activity, model for the degradation of the trp leader mRNA bound to TRAP. RNase J1 is the endonuclease cleaving scRNA that is 4 nts shorter on the 3' end Bacillus subtilis ?
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 ?
additional information the 5'-to-3' exoribonuclease activity of the enzyme is active on 5'-monophosphorylated or 5'-hydroxylated RNA requiring a single-stranded 5'-end, but is essentially completely inhibited by the triphosphorylated 5' ends of primary transcripts. The endonuclease activity is independent of the 5' phosphorylation status of the 5' end. The RNase J1/J2 complex has different endonucleolytic cleavage site preferences to the individual enzymes in vitro. RNase J2 has very poor 5'-to-3' exoribonuclease activity compared to RNase J1 Bacillus subtilis ?
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Synonyms

Synonyms Comment Organism
RNase J1
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 Bacillus subtilis
RNase J2
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 Bacillus subtilis

General Information

General Information Comment Organism
malfunction depletion of RNase J1 in a strain also lacking RNase J2 leads to a modest increase in global mRNA stability. transcriptome analysis shows a relatively minor effect of depleting cells for RNase J1 alone or inactivating RNase J2. The double mutant has altered levels for over 600 transcripts with about equal numbers of transcripts showing increased and decreased levels, significant increase in half-life for four specific transcripts cspC, spoVG, tagDccand yweA. Depletion of RNase J1 leads to an accumulation of 3' fragments of RNA Bacillus subtilis
physiological function role of enzymes RNase J1 and RNase J2 in both general and specific mRNA turnover, the enzymes RNase J1 and RNase J2 form a complex with 5'-to-3' exoribonuclease and endonucleolytic activity that plays a key role in the turnover and maturation of many RNAs in Bacillus subtilis. The 5'-to-3 exoribonuclease activity may be the more important of the complex's two modes of action. In addition to interacting with each other, RNase J1 and J2 might be part of a Bacillus subtilis degradosome complex containing two other ribonucleases, RNase Y and PNPase, phosphofructokinase and enolase Bacillus subtilis