- 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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 Abstract
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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
Citations to this article as recorded by  - 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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876
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Abstract
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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
- The α-Barrel Tip Region of Escherichia coli TolC Homologs of Vibrio vulnificus Interacts with the MacA Protein to Form the Functional Macrolide-Specific Efflux Pump MacAB-TolC
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Minho Lee , Hyun-Lee Kim , Saemee Song , Minju Joo , Seunghwa Lee , Daeyoung Kim , Yoonsoo Hahn , Nam-Chul Ha , Kangseok Lee
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J. Microbiol. 2013;51(2):154-159. Published online April 27, 2013
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DOI: https://doi.org/10.1007/s12275-013-2699-3
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821
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5
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20
Crossref
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Abstract
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TolC and its homologous family of proteins are outer membrane factors that are essential for exporting small molecules and toxins across the outer membrane in Gram-negative bacteria. Two open reading frames in the Vibrio vulnificus genome that encode proteins homologous to Escherichia coli TolC, designated TolCV1 and TolCV2, have 51.3% and 29.6% amino acid identity to TolC, respectively. In this study, we show that TolCV1 and TolCV2 functionally and physically interacted with the membrane fusion protein, MacA, a component of the macrolide-specific MacAB-TolC pump of E. coli. We further show that the conserved residues located at the aperture tip region of the α-hairpin of TolCV1 and TolCV2 played an essential role in the formation of the functional MacAB-TolC pump using site-directed mutational analyses. Our findings suggest that these outer membrane factors have
conserved tip-to-tip interaction with the MacA membrane fusion protein for action of the drug efflux pump in Gramnegative bacteria.
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Citations
Citations to this article as recorded by - Functions and Regulation of the Outer Membrane Protein TolC in Vibrio Species
Yue Gong, Chunxia Liu, Xin Tian, Young Ran Kim
ACS Infectious Diseases.2025; 11(7): 1756. CrossRef - ATP-binding cassette (ABC) transporters: structures and roles in bacterial pathogenesis
Shu Sian How, Sheila Nathan, Su Datt Lam, Sylvia Chieng
Journal of Zhejiang University-SCIENCE B.2025; 26(1): 58. CrossRef -
TolCV1 inhibition by NPPB renders
Vibrio vulnificus
less virulent and more susceptible to antibiotics
Yue Gong, Rui Jiang, Rui Hong Guo, Se Jin Jo, Hyeongju Jeong, Kyuho Moon, Joon Haeng Rhee, Young Ran Kim, Anne-Catrin Uhlemann
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and Type 1 Secretion Systems in Gram-Negative Bacteria
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