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서소진,김대영,송우석,허지훈,주민주,임예리,염지현,이강석 한국미생물학회 2017 The journal of microbiology Vol.55 No.1
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.
작은 여성에서 단일관튜브와 기관지 차단기를 사용한 일측 폐환기 -증례 보고-
서소진,임태완,손일순,김준현,홍덕만,강매화,전윤석,박재현 대한마취통증의학회 2010 Anesthesia and pain medicine Vol.5 No.2
One-lung ventilation with a double-lumen endotracheal tube or a UniventⓇ tube may be difficult or dangerous in small patients, children, and patients with anatomic abnormalities of the airway. The use of a bronchial blocker through a single-lumen endotracheal tube has been used successfully in such situations.A 69-year-old woman was scheduled for Ivor-Lewis operation and right upper lobectomy.She could not be intubated with a internal diameter 6.0 mm UniventⓇ tube owing to narrow diameter of the vocal cord. We report a successful one-lung ventilation using a UniblockerⓇ through an adult-size single-lumen endotracheal tube in a small woman, who needed postoperative ventilator care.
허지훈,서소진,이보은,염지현,이강석,Heo, Jihune,Seo, Sojin,Lee, Boeun,Yeom, Ji-Hyun,Lee, Kangseok The Microbiological Society of Korea 2016 미생물학회지 Vol.52 No.3
RNase E (Rne) is an essential enzyme involved in the processing and degradation of a large portion of RNAs in Escherichia coli. The enzymatic activity of RNase E is controlled by regulators of ribonuclease activity, namely, RraA and RraB. Gram-positive bacterium Streptomyces coelicolor also contains homologs of Rne and RraA, designated as RNase ES (Rns), RraAS1, and RraAS2. In the present study, we investigated the effect of S. coelicolor RraAS1 on the ribonucleolytic activity of RNase E in E. coli. Coexpression of RraAS1 with Rne resulted in the decreased levels of rpsO, ftsZ, and rnhB mRNAs, which are RNase E substrates, and augmented the toxic effect of Rne overexpression on cell growth. These in vivo effects appeared to be induced by the binding of RraAS1 to Rne, as indicated by the results of co-immunoprecipitation analysis. These results suggested that RraAS1 induces ribonucleolytic activity of RNase E in E. coli. RNase E는 대장균(Escherichia coli)에서 수많은 RNA의 가공 및 분해에 관여하는 필수적인 효소이다. RNase E의 효소 활성은 RraA와 RraB에 의해 조절된다. 그람양성균인 Streptomyces coelicolor는 RNase ES, RraAS1, RraAS2라고 명명되는 RNase E와 RraA의 동족체를 가지고 있다. 이 연구에서는 S. coelicolor 유래의 RraAS1이 E. coli에서 RNase E의 효소활성을 저해하는지 연구하였다. 대장균에서 RraAS1의 발현은 RNase E의 과발현에 의해 감소된 세포생장을 더욱 저하시켰으며, RNase E의 기질인 rpsO, ftsZ, rnhB mRNA의 양을 감소시키는 것을 확인 하였다. 이러한 RraAS1의 효과는 공동면역침전실험을 수행한 결과에서 유추할 수 있듯이, Rne 단백질과 RraAS1의 결합으로 유도되는 것으로 보인다. 이러한 결과는 RraAS1이 대장균에서 RNase E의 리보핵산 가수분해 활성을 유도함을 시사한다.
권영순,서소진,이상미 한국분석과학회 2002 분석과학 Vol.15 No.3
interfacial accumulation of the chromium-cupferron complex and the catalytic wave of its redox process is characterized by cyclic voltammetry. One cathodic peak is observed in the forward scan at -1.45 V. Scanning in the reverse direction produces a inverted peak at -1.39 V, which is indicative of a catalytic process. The optimal conditions of inverted peak were found to be 1 mM borate buffer solution(pH 9.48) containing 1×10-4 M cupferron, holding potential of -1.8 V and scan rate of 20 mV/s. Using main peak, a preconcentration time of 1 min results in a detection limit of 3.2×10-10 M.
허지훈,김대영,주민주,이보은,서소진,이재진,송새미,염지현,하남출,이강석 한국미생물학회 2016 The journal of microbiology Vol.54 No.10
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.