Functional Analysis of Vibrio vulnificus Orthologs of Escherichia coli RraA and RNase E

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• 作者：Daeyoung Kim ; Yong-Hak Kim ; Jinyang Jang ; Ji-Hyun Yeom…
• 刊名：Current Microbiology
• 出版年：2016
• 出版时间：June 2016
• 年：2016
• 卷：72
• 期：6
• 页码：716-722
• 全文大小：820 KB
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Microbiology
  Biotechnology
  
• 出版者：Springer New York
• ISSN：1432-0991
• 卷排序：72

文摘

RNase E plays an important role in the degradation and processing of RNA in Escherichia coli. The enzymatic activity of RNase E is controlled by the protein inhibitors RraA and RraB. The marine pathogenic bacterium Vibrio vulnificus also contains homologs of RNase E and RraA, designated as RNase EV, RraAV1, and RraAV2. Here, we report that RraAV1 actively inhibits the enzymatic activity of RNase EV in vivo and in vitro by interacting with the C-terminal domain of RNase EV. Coexpression of RraAV1 reduced ribonucleolytic activity in the cells overproducing RNase EV and consequently restored normal growth of these cells. An in vitro cleavage assay further demonstrated that RraAV1 efficiently inhibits the ribonucleolytic activity of RNase EV on BR10 + hpT, a synthetic oligonucleotide containing the RNase E cleavage site of RNA I. Our findings suggest that RraAV1 plays an active role in RNase EV-mediated RNA cleavage in V. vulnificus.Daeyoung Kim and Yong-Hak Kim have contributed equally to this work.