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Literature summary for 3.1.26.3 extracted from
- Characterization of ribonuclease III from Brucella (2016), Gene, 579, 183-192 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene rncS, DNA and amino acid sequence determination and analysis, sequence comparisons, Bm-RNase III is differently expressed in Brucella virulence strain 027 and vaccine strain M5-90 | Brucella melitensis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D61A | site-directed mutagenesis | Brucella melitensis |
| E133A | site-directed mutagenesis | Brucella melitensis |
| E54A | site-directed mutagenesis | Brucella melitensis |
| E81A | site-directed mutagenesis | Brucella melitensis |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Brucella melitensis |  |
| Mn2+ | required | Brucella melitensis | |
| additional information | cleavage activity of Bm-RNase III is bivalent metal cations-dependent | Brucella melitensis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Brucella melitensis | - |
isolated from an aborted goat | - |
| Brucella melitensis 027 | - |
isolated from an aborted goat | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | analysis of the ability of different metal ions and substrates to support the activity of RNase III in vitro, overview. Brucella melitensis sRNA and Homo sapiens pre-miRNAs as substrates: BM-pri-0015, BM-pre-0015, Has-let-7a-1, and Has-mir-16-1, transcripted by standard T7 transcription kit with [alpha-32P]-UTP labeling. BM-pri-0015 is 300 nt in length, while BM-pre-0015, Has-let-7a-1, and Has-mir-16-1 are about 70 nt. All the transcript sequences are featured with stem-loop structures. Bm-RNase III can not only bind prokaryotic sRNA, but also bind eukaryotic pre-miRNAs | Brucella melitensis | ? | - |
? | |
| additional information | analysis of the ability of different metal ions and substrates to support the activity of RNase III in vitro, overview. Brucella melitensis sRNA and Homo sapiens pre-miRNAs as substrates: BM-pri-0015, BM-pre-0015, Has-let-7a-1, and Has-mir-16-1, transcripted by standard T7 transcription kit with [alpha-32P]-UTP labeling. BM-pri-0015 is 300 nt in length, while BM-pre-0015, Has-let-7a-1, and Has-mir-16-1 are about 70 nt. All the transcript sequences are featured with stem-loop structures. Bm-RNase III can not only bind prokaryotic sRNA, but also bind eukaryotic pre-miRNAs | Brucella melitensis 027 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | three-dimensional structural model of Bm-RNase III based on homology modeling, best model structure is generated using 1o0w template from protein database, overview | Brucella melitensis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Bm-RNase III | - |
Brucella melitensis |
| RNase III | - |
Brucella melitensis |
| rncS | - |
Brucella melitensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Brucella melitensis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Brucella melitensis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
cleavage activity of Bm-RNase III is alkaline buffer-dependent | Brucella melitensis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme is a member of the RNase III superfamily | Brucella melitensis |
| malfunction | Bm-RNase III is differently expressed in Brucella virulence strain 027 and vaccine strain M5-90 | Brucella melitensis |
| additional information | cleavage activity of Bm-RNase III is bivalent metal cations- and alkaline buffer-dependent. Glu133 is required for catalytic activity. Three-dimensional structural model of Bm-RNase III based on homology modeling, overview | Brucella melitensis |
| physiological function | bacterial ribonuclease III (RNase III) is a highly conserved endonuclease, which plays pivotal roles in RNA maturation and decay pathways by cleaving double-stranded structure of RNAs. Brucella melitensis RNase III can efficiently bind and cleave stem-loop structure of small RNA, and might participate in regulation of virulence in Brucella. Brucella melitensis BM-pri-0015 and BM-pre-0015 containing double strand RNA structure, and Homo sapiens pre-miRNAs Hsa-let-7a-1 and Hsa-mir-16-1 obtained from miRBase are substrates of Bm-RNase III | Brucella melitensis |
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