- Crystal structure of Streptomyces coelicolor RraAS2, an unusual member of the RNase E inhibitor RraA protein family
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Nohra Park , Jihune Heo , Saemee Song , Inseong Jo , Kangseok Lee , Nam-Chul Ha
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J. Microbiol. 2017;55(5):388-395. Published online April 29, 2017
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DOI: https://doi.org/10.1007/s12275-017-7053-8
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Bacterial ribonuclease E (RNase E) plays a crucial role in the processing and decay of RNAs. A small protein named RraA negatively regulates the activity of RNase E via protein-protein interaction in various bacteria. Recently, RraAS1 and RraAS2, which are functional homologs of RraA from Escherichia coli, were identified in the Gram-positive species Streptomyces coelicolor. RraAS1 and RraAS2 inhibit RNase ES ribonuclease activity in S. coelicolor. RraAS1 and RraAS2 have a C-termi-nal extension region unlike typical bacterial RraA proteins. In this study, we present the crystal structure of RraAS2, ex-hibiting a hexamer arranged in a dimer of trimers, consistent with size exclusion chromatographic results. Importantly, the C-terminal extension region formed a long α-helix at the junction of the neighboring subunit, which is similar to the trimeric RraA orthologs from Saccharomyces cerevisiae. Trun-cation of the C-terminal extension region resulted in loss of RNase ES inhibition, demonstrating its crucial role. Our find-ings present the first bacterial RraA that has a hexameric assembly with a C-terminal extension α-helical region, which plays an essential role in the regulation of RNase ES activity in S. coelicolor.
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- S267P mutation of OxyR regulator in Zymomonas mobilis: mechanism of oxidative stress tolerance and applications in cellulosic hydrolysate fermentation and oxidative stress monitoring
Yi Wang, Binan Geng, Shuyi Liu, Yalun Wu, Shihui Yang Synthetic and Systems Biotechnology.2026; 13: 531. CrossRef - Relaxed Cleavage Specificity of Hyperactive Variants of Escherichia coli RNase E on RNA I
Dayeong Bae, Hana Hyeon, Eunkyoung Shin, Ji-Hyun Yeom, Kangseok Lee Journal of Microbiology.2023; 61(2): 211. CrossRef - An oxidative metabolic pathway of 4-deoxy-L-erythro-5-hexoseulose uronic acid (DEHU) from alginate in an alginate-assimilating bacterium
Ryuji Nishiyama, Takao Ojima, Yuki Ohnishi, Yasuhiro Kumaki, Tomoyasu Aizawa, Akira Inoue Communications Biology.2021;[Epub] CrossRef - The coordinated action of RNase III and RNase G controls enolase expression in response to oxygen availability in Escherichia coli
Minho Lee, Minju Joo, Minji Sim, Se-Hoon Sim, Hyun-Lee Kim, Jaejin Lee, Minkyung Ryu, Ji-Hyun Yeom, Yoonsoo Hahn, Nam-Chul Ha, Jang-Cheon Cho, Kangseok Lee Scientific Reports.2019;[Epub] CrossRef - RNase G controls tpiA mRNA abundance in response to oxygen availability in Escherichia coli
Jaejin Lee, Dong-Ho Lee, Che Ok Jeon, Kangseok Lee Journal of Microbiology.2019; 57(10): 910. 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
- RraAS1 inhibits the ribonucleolytic activity of RNase ES by interacting with its catalytic domain in Streptomyces coelicolor
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Sojin Seo , Daeyoung Kim , Wooseok Song , Jihune Heo , Minju Joo , Yeri Lim , Ji-Hyun Yeom , Kangseok Lee
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J. Microbiol. 2017;55(1):37-43. Published online December 30, 2016
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DOI: https://doi.org/10.1007/s12275-017-6518-0
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894
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RraA is a protein inhibitor of RNase E, which degrades and
processes numerous RNAs in Escherichia coli. Streptomyces
coelicolor also contains homologs of RNase E and RraA,
RNase ES and RraAS1/RraAS2, respectively. Here, we report
that, unlike other RraA homologs, RraAS1 directly interacts
with the catalytic domain of RNase ES to exert its inhibitory
effect. We further show that rraAS1 gene deletion in S. coelicolor
results in a higher growth rate and increased production
of actinorhodin and undecylprodigiosin, compared with
the wild-type strain, suggesting that RraAS1-mediated regulation
of RNase ES activity contributes to modulating the
cellular physiology of S. coelicolor.
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Citations
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- Translation as a regulatory hub for secondary metabolism in Streptomyces spp.
Francisco Barona-Gómez, Amelia Brave, Paul D. Straight Essays in Biochemistry.2026; 70(2): 187. CrossRef -
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 - The coordinated action of RNase III and RNase G controls enolase expression in response to oxygen availability in Escherichia coli
Minho Lee, Minju Joo, Minji Sim, Se-Hoon Sim, Hyun-Lee Kim, Jaejin Lee, Minkyung Ryu, Ji-Hyun Yeom, Yoonsoo Hahn, Nam-Chul Ha, Jang-Cheon Cho, Kangseok Lee Scientific Reports.2019;[Epub] CrossRef - RNase G controls tpiA mRNA abundance in response to oxygen availability in Escherichia coli
Jaejin Lee, Dong-Ho Lee, Che Ok Jeon, Kangseok Lee Journal of Microbiology.2019; 57(10): 910. 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
- RraAS2 requires both scaffold domains of RNase ES for high-affinity binding and inhibitory action on the ribonucleolytic activity
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Jihune Heo , Daeyoung Kim , Minju Joo , Boeun Lee , Sojin Seo , Jaejin Lee , Saemee Song , Ji-Hyun Yeom , Nam-Chul Ha , Kangseok Lee
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J. Microbiol. 2016;54(10):660-666. Published online September 30, 2016
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DOI: https://doi.org/10.1007/s12275-016-6417-9
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949
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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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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
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