Functional Conservation of RNase III-like Enzymes: Studies on a Vibrio vulnificus Ortholog of Escherichia coli RNase III
- Authors
- Lee, Minho; Ahn, Sangmi; Lim, Boram; Lee, Dong-Ho; Lee, Kangseok
- Issue Date
- Apr-2014
- Publisher
- SPRINGER
- Citation
- CURRENT MICROBIOLOGY, v.68, no.4, pp 413 - 418
- Pages
- 6
- Journal Title
- CURRENT MICROBIOLOGY
- Volume
- 68
- Number
- 4
- Start Page
- 413
- End Page
- 418
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/12332
- DOI
- 10.1007/s00284-013-0492-5
- ISSN
- 0343-8651
1432-0991
- Abstract
- Bacterial ribonuclease III (RNase III) belongs to the RNase III enzyme family, which plays a pivotal role in controlling mRNA stability and RNA processing in both prokaryotes and eukaryotes. In the Vibrio vulnificus genome, one open reading frame encodes a protein homologous to E. coli RNase III, designated Vv-RNase III, which has 77.9 % amino acid identity to E. coli RNase III. Here, we report that Vv-RNase III has the same cleavage specificity as E. coli RNase III in vivo and in vitro. Expressing Vv-RNase III in E. coli cells deleted for the RNase III gene (rnc) restored normal rRNA processing and, consequently, growth rates of these cells comparable to wild-type cells. In vitro cleavage assays further showed that Vv-RNase III has the same cleavage activity and specificity as E. coli RNase III on RNase III-targeted sequences of corA and mltD mRNA. Our findings suggest that RNase III-like proteins have conserved cleavage specificity across bacterial species.
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Collections - College of Natural Sciences > Department of Life Science > 1. Journal Articles
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