title: Functional Analysis of Vibrio vulnificus Orthologs of Escherichia coli RraA and RNase E.
abstract: 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.
authors.affiliation: Department of Life Science, Chung-Ang University, 84 Heukseok-ro, Dongjak-gu, Seoul, 06974, Republic of Korea.
authors.forename: Daeyoung
authors.initials: D
authors.lastname: Kim
authors.affiliation: Department of Microbiology, Catholic University of Daegu School of Medicine, 17 Duryugongwon-ro, Nam-gu, Taegu, 42472, Republic of Korea.
authors.forename: Yong-Hak
authors.initials: YH
authors.lastname: Kim
authors.affiliation: Department of Life Science, Chung-Ang University, 84 Heukseok-ro, Dongjak-gu, Seoul, 06974, Republic of Korea.
authors.forename: Jinyang
authors.initials: J
authors.lastname: Jang
authors.affiliation: Department of Life Science, Chung-Ang University, 84 Heukseok-ro, Dongjak-gu, Seoul, 06974, Republic of Korea.
authors.forename: Ji-Hyun
authors.initials: JH
authors.lastname: Yeom
authors.affiliation: Department of Life Science, Chung-Ang University, 84 Heukseok-ro, Dongjak-gu, Seoul, 06974, Republic of Korea.
authors.forename: Jong Woo
authors.initials: JW
authors.lastname: Jun
authors.affiliation: Department of Life Science, Chung-Ang University, 84 Heukseok-ro, Dongjak-gu, Seoul, 06974, Republic of Korea. sghyun@cau.ac.kr.
authors.forename: Seogang
authors.initials: S
authors.lastname: Hyun
authors.affiliation: Department of Life Science, Chung-Ang University, 84 Heukseok-ro, Dongjak-gu, Seoul, 06974, Republic of Korea. kangseok@cau.ac.kr.
authors.forename: Kangseok
authors.initials: K
authors.lastname: Lee
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D004722:Endoribonucleases / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D012329:RNA, Bacterial / Q000235:genetics / Q000378:metabolism; D041261:Vibrio vulnificus / Q000201:enzymology* / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D012329:RNA, Bacterial; C477942:RraA protein, E coli; D004722:Endoribonucleases; C022537:ribonuclease E