EC Number   |
General Information |
Reference  |
|---|
   4.6.1.22 | physiological function |
RNase J1 is essential, while its paralogue RNase J2 is not. RNases J1 and J2 form a complex that is likely to be the predominant form of these enzymes in wild-type cells: RNase J2 co-purifies with His-tagged RNase J1 from Escherichia coli or with Flag-tagged RNase J1 from Bacillus subtilis and RNases J1 and J2 interact in vivo in a yeast two-hybrid assay. While both RNase J1 and the RNase J1/J2 complex have robust 5'-to-3' exoribonuclease activity in vitro, RNase J2 has at least two orders of magnitude weaker exonuclease activity. Association of the two proteins also has an effect on the endoribonucleolytic properties of RNases J1 and J2. While the individual enzymes have similar endonucleolytic cleavage activities and specificities, as a complex they behave synergistically to alter cleavage site preference and to increase cleavage efficiency at specific sites |
710000 |
| 4.6.1.22 | malfunction |
DELTAermC mRNA shows increased stability in a RNase J1 mutant strain, that contains reduced level of RNase J1. Insertion of a strong stem-loop structure at +65 results in increased stability. Weakening this stem-loop structure results in reversion to wild-type stability. RNA fragments containing the 3' end are detected in a strain with reduced RNase J1 expression, but are undetectable in the wild-type. The 5' ends of these fragments map to the upstream side of predicted stem-loop structures, consistent with an impediment to RNase J1 5' exonuclease processivity. RNase J1 is involved even in decay of the RNA encoded by a 129-nt deletion construct, perhaps by a 59-to-39 exonucleolytic pathway or by cleavage at sites in the upstream half of the RNA. Deletion of the three target sites results in increased mRNA half-life (ca. 15 min) |
710551 |
| 4.6.1.22 | more |
the enzyme is conformationally heterogeneous and folds with multiphasic kinetics, indicating the presence of an equilibrium and kinetic intermediate in its folding mechanism, NMR spectroscopy analysis, overview. RNase P protein is the protein subunit in the RNase P ribonucleoholoenzyme, it is an intrinsically disordered protein. Without the binding partners, P protein is predominantly unfolded but can be induced to fold in the presence of different small anions, e.g. sulfate. The N-terminal and C-terminal helical regions are mostly unfolded in the intermediate. The protonation of His22 may play a major role in the energetics of the equilibria between the unfolded, intermediate, and folded state ensembles of P protein, possible role for the intermediate in the enzyme holoenzyme assembly process. HSQC spectrum of folded P protein and unfolded P protein, overview |
729206 |
| 4.6.1.22 | malfunction |
rpsO mRNA half-life is unchanged in a strain that has decreased RNase J1 activity and no RNase J2 activity, but it is 2.3fold higher in a strain with decreased activity of RNase Y |
729917 |
| 4.6.1.22 | metabolism |
Bacillus subtilis endonucleases Bs-RNase III, RNase M5, RNase P, RNase Z, EndoA, and Mini-III are not involved in rpsO mRNA decay, the upstream products are degraded by polynucleotide phosphorylase (PNPase), and the downstream products were degraded by the 5' exonuclease activity of RNase J1 |
729917 |
| 4.6.1.22 | physiological function |
RNase Y mediates the initiation of rpsO mRNA decay, the stability of the specific mRNA is determined by RNase Y |
729917 |
| 4.6.1.22 | physiological function |
in Bacillus subtilis, the dual activity 5' exo- and endoribonucleases J1 and J2 are important players in mRNA and stable RNA maturation and degradation. The two nucleases in the cell primarily act as a heterodimer in vivo |
-, 729939 |
| 4.6.1.22 | malfunction |
lowering RNase Y concentration may affect RNA decay indirectly via an effect on RNase J1, which is thought to exist with RNase Y in a degradosome complex |
-, 729973 |
| 4.6.1.22 | physiological function |
endonucleolytic cleavage by ribonuclease RNase J1 in a 3'-proximal, single-stranded regionis critical for initiation of trp leader RNA decay, the enzyme accesses its internal target site on trp leader RNA in a 5' end-independent manner. The mechanism of trp leader RNA decay is not dependent on TRAP binding |
-, 729973 |
| 4.6.1.22 | evolution |
the enzyme belongs to the beta-CASP subfamily of metallo-beta-lactamases |
730404 |
