EC Number   |
General Information |
Reference |
|---|
   4.6.1.22 | more |
modeling of the enzyme reaction involving the binding of the RNA to the surface of the beta-CASP domain to explain the enzyme's processive action, enzyme residues involved in RNA recognition, RNA-binding channel and proposed nucleotide Exit tunnel of RNase J, modeling, overview |
730975 |
| 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 | 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 | physiological function |
enzyme RNase J has been shown to play an extensive role in mRNA turnover. The bifunctional 5'-3' exo/endoribonuclease RNase J is involved in the maturation and turnover of RNAs in prokaryotes |
730975 |
| 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 | physiological function |
ribonucleases J1 and J2 participate in degradation and regulatory processing of mRNA. mRNA decay is important in regulation of virulence factors of Streptococcus pyogenes, both of these RNases are essential for growth of the organism. RNases J1 and J2 affect the rate of decay of class I messages and the length of the first phase in decay of class II messages, overview |
730404 |
| 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 | physiological function |
RNase Y is a key endoribonuclease affecting global mRNA stability in Bacillus subtilis, in which endonucleolytic cleavage plays a major role in the mRNA metabolism, it plays a key role in initiating the decay of a large number of mRNAs as well as non coding RNAs |
730720 |
| 4.6.1.22 | physiological function |
RNase Y is an endoribonuclease affecting global mRNA metabolism, it affects the expression of the Bacillus subtilis infCrpmI-rplT operon, encoding translation initiation factor IF3 and the ribosomal proteins L35 and L20, which is an operon autoregulated by a complex L20-dependent transcription attenuation mechanism. The readthrough transcript of a second promoter P1, upstream of the promoter P2, is stabilized in a strain depleted for RNase Y, while the readthrough transcript of P2 is not. Under these conditions infC biosynthesis is repressed threefold, regulatory model for the control of the Bacillus subtilis infC operon, overview |
-, 730409 |
| 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 |
