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Literature summary extracted from

  • Wu, C.X.; Xu, X.J.; Zheng, K.; Liu, F.; Yang, X.D.; Chen, C.F.; Chen, H.C.; Liu, Z.F.
    Characterization of ribonuclease III from Brucella (2016), Gene, 579, 183-192 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.26.3 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

EC Number Protein Variants Comment Organism
3.1.26.3 D61A site-directed mutagenesis Brucella melitensis
3.1.26.3 E133A site-directed mutagenesis Brucella melitensis
3.1.26.3 E54A site-directed mutagenesis Brucella melitensis
3.1.26.3 E81A site-directed mutagenesis Brucella melitensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.26.3 Mg2+ required Brucella melitensis
3.1.26.3 Mn2+ required Brucella melitensis
3.1.26.3 additional information cleavage activity of Bm-RNase III is bivalent metal cations-dependent Brucella melitensis

Organism

EC Number Organism UniProt Comment Textmining
3.1.26.3 Brucella melitensis
-
 isolated from an aborted goat
-
3.1.26.3 Brucella melitensis 027
-
 isolated from an aborted goat
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.26.3 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 ?
-
 ?
3.1.26.3 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

EC Number Subunits Comment Organism
3.1.26.3 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

EC Number Synonyms Comment Organism
3.1.26.3 Bm-RNase III
-
 Brucella melitensis
3.1.26.3 RNase III
-
 Brucella melitensis
3.1.26.3 rncS
-
 Brucella melitensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.26.3 37
-
 assay at Brucella melitensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.26.3 8
-
 assay at Brucella melitensis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.26.3 additional information
-
 cleavage activity of Bm-RNase III is alkaline buffer-dependent Brucella melitensis

General Information

EC Number General Information Comment Organism
3.1.26.3 evolution the enzyme is a member of the RNase III superfamily Brucella melitensis
3.1.26.3 malfunction Bm-RNase III is differently expressed in Brucella virulence strain 027 and vaccine strain M5-90 Brucella melitensis
3.1.26.3 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
3.1.26.3 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