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HOME > J. Microbiol > Volume 54(10); 2016 > Article
Journal Article
RraAS2 requires both scaffold domains of RNase ES for high-affinity binding and inhibitory action on the ribonucleolytic activity
Jihune Heo 1, Daeyoung Kim 1, Minju Joo 1, Boeun Lee 1, Sojin Seo 1, Jaejin Lee 1, Saemee Song 2, Ji-Hyun Yeom 1, Nam-Chul Ha 2, Kangseok Lee 1
Journal of Microbiology 2016;54(10):660-666.
DOI: https://doi.org/10.1007/s12275-016-6417-9
Published online: September 30, 2016
1Department of Life Science, Chung-Ang University, Seoul 06974, Republic of Korea, 2Department of Agricultural Biotechnology, Seoul National University, Seoul 08826, Republic of Korea1Department of Life Science, Chung-Ang University, Seoul 06974, Republic of Korea, 2Department of Agricultural Biotechnology, Seoul National University, Seoul 08826, Republic of Korea
Corresponding author:  Kangseok Lee , Tel: -, 
Received: 25 August 2016   • Revised: 7 September 2016   • Accepted: 7 September 2016
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Abstract

RraA is a protein inhibitor of RNase E (Rne), which catalyzes the endoribonucleolytic cleavage of a large proportion of RNAs in Escherichia coli. The antibiotic‐producing bacterium Streptomyces coelicolor also contains homologs of RNase E and RraA, designated as RNase ES (Rns), RraAS1, and RraAS2, respectively. Here, we report that RraAS2 requires both scaffold domains of RNase ES for high-affinity binding and inhibitory action on the ribonucleolytic activity. Analyses of the steady-state level of RNase E substrates indicated that coexpression of RraAS2 in E. coli cells overproducing Rns effectively inhibits the ribonucleolytic activity of full-length RNase ES, but its inhibitory effects were moderate or undetectable on other truncated forms of Rns, in which the N- or/and C-terminal scaffold domain was deleted. In addition, RraAS2 more efficiently inhibited the in vitro ribonucleolytic activity of RNase ES than that of a truncated form containing the catalytic domain only. Coimmunoprecipitation and in vivo cross-linking experiments further showed necessity of both scaffold domains of RNase ES for high-affinity binding of RraAS2 to the enzyme, resulting in decreased RNA-binding capacity of RNase ES. Our results indicate that RraAS2 is a protein inhibitor of RNase ES and provide clues to how this inhibitor affects the ribonucleolytic activity of RNase ES.

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    RraAS2 requires both scaffold domains of RNase ES for high-affinity binding and inhibitory action on the ribonucleolytic activity
    J. Microbiol. 2016;54(10):660-666.   Published online September 30, 2016
    DOI: https://doi.org/10.1007/s12275-016-6417-9
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