Sinorhizobium meliloti RNase III: Catalytic Features and Impact on Symbiosis

Frontiers in Genetics
Margarida SaramagoCecília M Arraiano

Abstract

Members of the ribonuclease (RNase) III family of enzymes are metal-dependent double-strand specific endoribonucleases. They are ubiquitously found and eukaryotic RNase III-like enzymes include Dicer and Drosha, involved in RNA processing and RNA interference. In this work, we have addressed the primary characterization of RNase III from the symbiotic nitrogen-fixing α-proteobacterium Sinorhizobium meliloti. The S. meliloti rnc gene does encode an RNase III-like protein (SmRNase III), with recognizable catalytic and double-stranded RNA (dsRNA)-binding domains that clusters in a branch with its α-proteobacterial counterparts. Purified SmRNase III dimerizes, is active at neutral to alkaline pH and behaves as a strict metal cofactor-dependent double-strand endoribonuclease, with catalytic features distinguishable from those of the prototypical member of the family, the Escherichia coli ortholog (EcRNase III). SmRNase III prefers Mn2+ rather than Mg2+ as metal cofactor, cleaves the generic structured R1.1 substrate at a site atypical for RNase III cleavage, and requires higher cofactor concentrations and longer dsRNA substrates than EcRNase III for optimal activity. Furthermore, the ultraconserved E125 amino acid was shown to play ...Continue Reading

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Citations

Apr 18, 2019·Nucleic Acids Research·Hendrik MeliorElena Evguenieva-Hackenberg
Oct 23, 2020·Environmental Microbiology·Patrícia ApuraSandra C Viegas
Aug 25, 2021·Microbial Biotechnology·Patrícia ApuraCecília M Arraiano

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Methods Mentioned

BETA
PCRs
PCR
gel filtration
in vitro transcription
in
electrophoresis

Software Mentioned

ClustalW2
Phylogeny
ImageQuant
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