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  • 08월 28일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

Histone H3 N-Terminal Peptide Directly Binds to Its Own mRNA: a Possible Mode of Feedback Inhibition to Control Translation

등록일
2008년 8월 6일 18시 20분 08초
접수번호
0204
발표코드
33P167포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅰ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
이경현, 현순실, 유재훈
서울대학교 화학교육과, Korea
Histone protein is one of the most abundant proteins in cells and its concentration is closely governed during cell cycle. Early reports describing histone auto-regulation suggested that a complex of histone proteins and its cognate mRNA is involved in reducing histone levels. In order to uncover the cis-element for auto-regulation, SELEX against histone H3 peptide was carried out. Notably, selected aptamers provided specific hairpin motif, which possess high homology with histone H3 mRNA. BLAST search of these sequences identified other histone related mRNAs containing homologous sequences of hairpin motif, as a potent target motif for histone H3 protein. Identified H3 hairpin RNA specifically binds to H3 peptide with micromolar affinity. Moreover, in vitro translation of H3 protein is inhibited in a dose-dependent manner by the H3 N-terminal peptide and addition of H3 hairpin RNA restored H3 protein expression. Taken together, these results suggested that the pair comprised of hairpin RNA in H3 mRNA and the cognate histone H3 protein is one of the rare cis-elements on coding region for feedback regulation.

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