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박노라,허지훈,송새미,조인성,이강석,하남출 한국미생물학회 2017 The journal of microbiology Vol.55 No.5
Bacterial ribonuclease E (RNase E) plays a crucial role in theprocessing and decay of RNAs. A small protein named RraAnegatively regulates the activity of RNase E via protein-proteininteraction in various bacteria. Recently, RraAS1 and RraAS2,which are functional homologs of RraA from Escherichia coli,were identified in the Gram-positive species Streptomycescoelicolor. RraAS1 and RraAS2 inhibit RNase ES ribonucleaseactivity in S. coelicolor. RraAS1 and RraAS2 have a C-terminalextension region unlike typical bacterial RraA proteins. In this study, we present the crystal structure of RraAS2, exhibitinga hexamer arranged in a dimer of trimers, consistentwith size exclusion chromatographic results. Importantly,the C-terminal extension region formed a long α-helix at thejunction of the neighboring subunit, which is similar to thetrimeric RraA orthologs from Saccharomyces cerevisiae. Truncationof the C-terminal extension region resulted in loss ofRNase ES inhibition, demonstrating its crucial role. Our findingspresent the first bacterial RraA that has a hexamericassembly with a C-terminal extension α-helical region, whichplays an essential role in the regulation of RNase ES activityin S. coelicolor.
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박노라,송새미,최가람,장경구,조인성,최상호,하남출 한국분자세포생물학회 2017 Molecules and cells Vol.40 No.4
The transcriptional activator AphB has been implicated in acid resistance and pathogenesis in the food borne pathogens Vibrio vulnificus and Vibrio cholerae. To date, the full-length AphB crystal structure of V. cholerae has been determined and characterized by a tetrameric assembly of AphB consisting of a DNA binding domain and a regulatory domain (RD). Although acidic pH and low oxygen tension might be in-volved in the activation of AphB, it remains unknown which ligand or stimulus activates AphB at the molecular level. In this study, we determine the crystal structure of the AphB RD from V. vulnificus under aerobic conditions without modification at the conserved cysteine residue of the RD, even in the presence of the oxidizing agent cumene hydroperoxide. A cysteine to serine amino acid residue mutant RD protein further confirmed that the cysteine residue is not involved in sensing oxidative stress in vitro. Interestingly, an unidentified small molecule was observed in the inter-subdomain cavity in the RD when the crystal was incubated with cumene hydroperoxide molecules, suggesting a new ligand-binding site. In addition, we confirmed the role of AphB in acid tolerance by observing an aphB-dependent in-crease in cadC transcript level when V. vulnificus was exposed to acidic pH. Our study contributes to the understanding of the AphB molecular mechanism in the process of recognizing the host environment.
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