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| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Exhibition Hall 2+3 |
| Time |
10월 19일 (목요일) 11:00~12:30 |
| Code |
BIO.P-287 |
| Subject |
Structural and functional characterization of a wobble uridine modifying enzyme from Mycobacterium tuberculosis |
| Authors |
sanghyun lee, Jungwook Kim1,*
department of chemistry, Gwangju Institute of Science and Technology, Korea
1Department of Chemistry, Gwangju Institute of Science and Technology, Korea
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| Abstract |
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. |
| E-mail |
leeshanghyun@naver.com |
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120th General Meeting of the KCS