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Literature summary for 3.1.26.3 extracted from

  • Lioliou, E.; Sharma, C.M.; Caldelari, I.; Helfer, A.C.; Fechter, P.; Vandenesch, F.; Vogel, J.; Romby, P.
    Global regulatory functions of the Staphylococcus aureus endoribonuclease III in gene expression (2012), PLoS Genet., 8, e1002782.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene mc, DNA and amino acid sequence determination and analysis Staphylococcus aureus

Protein Variants

Protein Variants Comment Organism
D63A site-directed mutagenesis, analysis of binding specificity and target sites compared to the wild-type enzyme Staphylococcus aureus
E135A site-directed mutagenesis, analysis of binding specificity and target sites compared to the wild-type enzyme Staphylococcus aureus
additional information effect of mutations in the catalytic site of Staphylococcus aureus RNase III, overview Staphylococcus aureus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Staphylococcus aureus enzyme RNase III cleavage produces RNA fragments with 5'-phosphate and 3'-hydroxyl termini and a two-nucleotide 3'-overhang. The 5' untranslated region of cspA mRNA is processed by the enzyme. Determination of substrate specificity by sequencing on cDNA libraries generated from RNAs that are co-immunoprecipitated with wild-type RNase III or two different cleavage-defective mutant variants D63A and E135A in vivo, validation of several RNA targets and mapping of cleavage sites of wild-type and mutant enzymes, detailed overview ?
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additional information Staphylococcus aureus RN6390 enzyme RNase III cleavage produces RNA fragments with 5'-phosphate and 3'-hydroxyl termini and a two-nucleotide 3'-overhang. The 5' untranslated region of cspA mRNA is processed by the enzyme. Determination of substrate specificity by sequencing on cDNA libraries generated from RNAs that are co-immunoprecipitated with wild-type RNase III or two different cleavage-defective mutant variants D63A and E135A in vivo, validation of several RNA targets and mapping of cleavage sites of wild-type and mutant enzymes, detailed overview ?
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Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
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gene mc
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Staphylococcus aureus RN6390
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gene mc
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme RNase III cleavage produces RNA fragments with 5'-phosphate and 3'-hydroxyl termini and a two-nucleotide 3'-overhang. The 5' untranslated region of cspA mRNA is processed by the enzyme. Determination of substrate specificity by sequencing on cDNA libraries generated from RNAs that are co-immunoprecipitated with wild-type RNase III or two different cleavage-defective mutant variants D63A and E135A in vivo, validation of several RNA targets and mapping of cleavage sites of wild-type and mutant enzymes, detailed overview Staphylococcus aureus ?
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additional information enzyme RNase III cleavage produces RNA fragments with 5'-phosphate and 3'-hydroxyl termini and a two-nucleotide 3'-overhang. The 5' untranslated region of cspA mRNA is processed by the enzyme. Determination of substrate specificity by sequencing on cDNA libraries generated from RNAs that are co-immunoprecipitated with wild-type RNase III or two different cleavage-defective mutant variants D63A and E135A in vivo, validation of several RNA targets and mapping of cleavage sites of wild-type and mutant enzymes, detailed overview Staphylococcus aureus RN6390 ?
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Synonyms

Synonyms Comment Organism
endoribonuclease III
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Staphylococcus aureus
RNase III
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Staphylococcus aureus

General Information

General Information Comment Organism
evolution the enzyme RNase III is a member of the ubiquitous family of double-strand-specific endoribonucleases Staphylococcus aureus
additional information the enzyme autoregulates its own expression. Contributions of residues E135 and D63 to the active site of the enzyme Staphylococcus aureus
physiological function the enzyme has a broad function in gene regulation in response to stress and during host infection of Staphylococcus aureus. RNase III-mediated cleavage in the 5' untranslated region enhances the stability and translation of cspA mRNA, which encodes the major cold-shock protein. Processing of cspA mRNA by the enzyme activates CspA synthesis. RNase III cleaves overlapping 5'-UTRs of divergently transcribed genes to generate leaderless mRNAs, which constitutes a distinct way to co-regulate neighboring genes. RNase III initiates maturation of rRNA operons. In addition to gene regulation, the enzyme is associated with RNA quality control of pervasive transcription, complexity of post-transcriptional regulation mediated by RNase III, possible function of the enzyme in the decay of structured regions of mRNAs, overview Staphylococcus aureus