Sphingorhabdus sp. YGSMI21, a novel microbial strain with
an enantioselective epoxide hydrolase activity, was isolated
from tidal samples contaminated by accidental oil spills subjected
to enriched culture with polycyclic aromatic hydrocarbon.
This strain was able to optically decompose (R)-styrene
oxide (SO) and showed 100% optical purity. In addition, it
showed a good enantioselectivity for the derivatives of (S)-
SO, (S)-2-chlorostyrene oxide (CSO), (S)-3-CSO and (S)-4-
CSO. For (S)-2-CSO, (S)-3-CSO and (S)-4-CSO, 99.9%ee was
obtained with the yield of 26.2%, 24.8%, and 11.0%, respectively,
when using 10 mg cells of Sphingorhabdus sp. YGSMI21
at pH 8.0 with 4 mM racemic substrates at pH 8.0 and 25°C.
The values obtained in this study for (S)-2-CSO, particularly
the yield of 26.2%, is noteworthy, considering that obtaining
an enantiomerically pure form is difficult. Taken together,
Sphingorhabdus sp. YGSMI21 can be regarded as a wholecell
biocatalyst in the production of various (S)-CSO with the
chlorine group at a different position.
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Epoxide Hydrolases: Multipotential Biocatalysts Marek Bučko, Katarína Kaniaková, Helena Hronská, Peter Gemeiner, Michal Rosenberg International Journal of Molecular Sciences.2023; 24(8): 7334. CrossRef
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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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Identification of the global regulatory roles of RraA via the integrative transcriptome and proteome in
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Huizhen Chen, Qian Gao, Bing Liu, Ying Zhang, Jianxiang Fang, Songbiao Wang, Youqi Chen, Chang Chen, Nicolas E. Buchler mSphere.2024;[Epub] CrossRef
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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
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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.
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
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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