RraAS2 requires both scaffold domains of RNase ES for high-affinity binding and inhibitory action on the ribonucleolytic activity

Jihune Heo; Daeyoung Kim; Minju Joo; Boeun Lee; Sojin Seo; Jaejin Lee; Saemee Song; Ji-Hyun Yeom; Nam-Chul Ha; Kangseok Lee

doi:10.1007/s12275-016-6417-9

Articles

Page Path: 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

prev next

50 Views
0 Download
9 Crossref
9 Scopus

Full Article

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.

Keywords: Streptomyces coelicolor;RNA stability;RNase ES;RraAS2

Figure & Data

References

Citations

Citations to this article as recorded by

Identification of the global regulatory roles of RraA via the integrative transcriptome and proteome in Vibrio alginolyticus
Huizhen Chen, Qian Gao, Bing Liu, Ying Zhang, Jianxiang Fang, Songbiao Wang, Youqi Chen, Chang Chen, Nicolas E. Buchler
mSphere.2024;[Epub] CrossRef
Streptomyces RNases – Function and impact on antibiotic synthesis
George H. Jones
Frontiers in Microbiology.2023;[Epub] CrossRef
Regulator of RNase E activity modulates the pathogenicity of Salmonella Typhimurium
Jaejin Lee, Eunkyoung Shin, Ji-Hyun Yeom, Jaeyoung Park, Sunwoo Kim, Minho Lee, Kangseok Lee
Microbial Pathogenesis.2022; 165: 105460. CrossRef
Regulator of ribonuclease activity modulates the pathogenicity of Vibrio vulnificus
Jaejin Lee, Eunkyoung Shin, Jaeyeong Park, Minho Lee, Kangseok Lee
Journal of Microbiology.2021; 59(12): 1133. CrossRef
Divergent rRNAs as regulators of gene expression at the ribosome level
Wooseok Song, Minju Joo, Ji-Hyun Yeom, Eunkyoung Shin, Minho Lee, Hyung-Kyoon Choi, Jihwan Hwang, Yong-In Kim, Ramin Seo, J. Eugene Lee, Christopher J. Moore, Yong-Hak Kim, Seong-il Eyun, Yoonsoo Hahn, Jeehyeon Bae, Kangseok Lee
Nature Microbiology.2019; 4(3): 515. CrossRef
RraAS1 inhibits the ribonucleolytic activity of RNase ES by interacting with its catalytic domain in Streptomyces coelicolor
Sojin Seo, Daeyoung Kim, Wooseok Song, Jihune Heo, Minju Joo, Yeri Lim, Ji-Hyun Yeom, Kangseok Lee
Journal of Microbiology.2017; 55(1): 37. CrossRef
Bdm-Mediated Regulation of Flagellar Biogenesis in Escherichia coli and Salmonella enterica Serovar Typhimurium
Jaejin Lee, Dae-Jun Kim, Ji-Hyun Yeom, Kangseok Lee
Current Microbiology.2017; 74(9): 1015. CrossRef
Functional implications of hexameric assembly of RraA proteins from Vibrio vulnificus
Saemee Song, Seokho Hong, Jinyang Jang, Ji-Hyun Yeom, Nohra Park, Jaejin Lee, Yeri Lim, Jun-Yeong Jeon, Hyung-Kyoon Choi, Minho Lee, Nam-Chul Ha, Kangseok Lee, Eric Cascales
PLOS ONE.2017; 12(12): e0190064. CrossRef
Crystal structure of Streptomyces coelicolor RraAS2, an unusual member of the RNase E inhibitor RraA protein family
Nohra Park, Jihune Heo, Saemee Song, Inseong Jo, Kangseok Lee, Nam-Chul Ha
Journal of Microbiology.2017; 55(5): 388. CrossRef

Cite this Article

Cite this Article: export Copy Download Format; Close

Download Citation

Download a citation file in RIS format that can be imported by all major citation management software, including EndNote, ProCite, RefWorks, and Reference Manager.

Format:

RIS — For EndNote, ProCite, RefWorks, and most other reference management software
BibTeX — For JabRef, BibDesk, and other BibTeX-specific software

Include:

Citation for the content below
Citation and abstract for the content below

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

Related articles