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제120회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Structural and functional characterization of a wobble uridine modifying enzyme from Mycobacterium tuberculosis

등록일
2017년 8월 31일 15시 36분 16초
접수번호
2409
발표코드
BIO.P-287 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
10월 19일 (목요일) 11:00~12:30
발표형식
포스터
발표분야
Life Chemistry
저자 및
공동저자
sanghyun lee, Jungwook Kim1,*
department of chemistry, Gwangju Institute of Science and Technology, Korea
1Department of Chemistry, Gwangju Institute of Science and Technology, Korea
To date, ~140 modified nucleosides have been identified in RNA, where most of them are observed among tRNA. These post-transcriptional modifications are formed via enzymatic reactions, and the list of such RNA modifying activity is still expanding. Recently, our laboratory has discovered a novel O-methyl transferase, YrrM, acting on tRNA in Bacillus subtilis. The enzyme directs the methylation of hypomodified wobble uridine (5-hydroxyuridine) on several isoacceptors in Gram-positive bacteria. The homologous search led us to identify a candidate enzyme from MTB, which shares ~38% (CHECK!) sequence identity with B. subtilis YrrM. Here we present the X-ray crystal structure and in vitro data of the MTB O-methyltransferase, supporting its role in tRNA modification.

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