Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
gene rnc | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | txpA and RatA form an extended hybrid that is a substrate for RNase III cleavage | Bacillus subtilis | ? | - |
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Synonyms | Comment | Organism |
---|---|---|
RNase III | - |
Bacillus subtilis |
General Information | Comment | Organism |
---|---|---|
malfunction | in the absence of RNase III, only trace amounts of 30S rRNA precursor are observed in Bacillus subtilis. A significant increase in the steady-state levels of the type I toxin mRNA txpA occurs in strains depleted for RNase III. Expression of the txpA and yonT toxin mRNAs account for the lethality of the Skin and SPbeta prophages in RNase III mutants | Bacillus subtilis |
metabolism | the enzymes that catalyze the final steps of rRNA maturation, RNase J1, Mini-III and RNase M5, function efficiently without prior RNase III action | Bacillus subtilis |
physiological function | the enzyme plays a role in the mechanism of RatA mediated degradation of txpA mRNA both in vivo and in vitro and in cleaving double-stranded RNA in many biological systems, it is involved in ribosomal RNA maturation and mRNA turnover. In contrast to other bacteria, the enzyme is essential in Bacillus subtilis, it protects the organism from the expression of toxin genes borne by two prophages, through antisense RNA, although it is not responsible for the stabilities of antisense-RNAs. Degradation of type I toxin txpA is dependent on both RatA and RNase III. The organism uses RNase III or its homologues as part of viral defense or viral accommodation mechanisms | Bacillus subtilis |