EC Number   |
Natural Substrates |
|---|
   4.6.1.22 | more |
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 |
| 4.6.1.22 | more |
ribonucleases J1 and J2 have both endoribonucleolytic and 5'-to-3' exoribonucleolytic activities. Both act on class I and class II mRNAs, overview |
| 4.6.1.22 | more |
RNase J is a bifunctional 5'-3' exo/endoribonuclease |
| 4.6.1.22 | more |
RNase J is a bifunctional 5'-3' exo/endoribonuclease, structure of enzyme bound to a 4-nucleotide RNA showing an RNA-binding channel. A second, negatively charged tunnel leads from the active site, and is ideally located to evacuate the cleaved nucleotide in 5'-3' exonucleolytic mode |
| 4.6.1.22 | more |
RNase J1 is a dual-specificity enzyme, with both 5' exonucleolytic and endonucleolytic activities. 5'-SSS RNA is unlikely to be a good substrate for 5' exonucleolytic attack in vivo |
| 4.6.1.22 | more |
the enzyme degrades of a large number of mRNAs as well as non coding RNAs |
| 4.6.1.22 | RNA + H2O |
- |
| 4.6.1.22 | rpsO mRNA + H2O |
aspects of mRNA decay initiation in Bacillus subtilis. Endonuclease cleavage in the body of the message, rather than degradation from the native 3' end, is the rate-determining step for mRNA decay |
| 4.6.1.22 | trp leader RNA + H2O |
endonucleolytic cleavage by ribonuclease RNase J1 in a 3'-proximal, single-stranded region. trp leader RNA is a small (140-nucleotide) RNA that results from attenuation of trp operon transcription upon binding of the regulatory TRAP complex. In the RNase J1 mutant strain, trp:rpsO-TT RNA half-life increases 2.3fold to 8.2 min |
