abs

학술발표회초록보기

초록문의 abstract@kcsnet.or.kr

결제문의 member@kcsnet.or.kr

현재 가능한 작업은 아래와 같습니다.
  • 08월 28일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

The roles of α-helix1 in HSF1 DNA-binding domain during the heat-activation

등록일
2008년 8월 11일 11시 10분 21초
접수번호
0482
발표코드
33P184포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅰ>
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
Ming Lu, 이윤주1, 박성민1, 박장수1
부산대학교 화학과, China
1부산대학교 화학과, Korea
Human heat shock transcription factor 1 (HSF1) is a major transcriptional regulator in the heat shock response. However, the roles of α-helix1 (H1) in the DNA-binding domain (DBD) of HSF1 are still unknown. In our study, removal of H1 could result in loss of heat-induced activities, suggesting the importance of H1 in HSF1-activation. H1 contains two highly conserved aromatic amino acids (Phe18 and Trp23). Mutations of these two amino acids reduce HSF1 DNA-binding activity. Three-dimensional structure of HSF DBD by X-ray spectroscopy showed that Phe18 and Trp23 could contact with other aromatic amino acids in DNA-binding domain. From our results, mutations of Tyr60 and Phe104 also showed the lower heat-induced activities than WT HSF1. We presume that H1 might be involved in hHSF1-activation: H1 contains an amphipathic right-handed helix. Deletion of H1 breaks down the thermal stability. Thus under heat stress condition, HSF1 mutant can not form trimer and show the DNA-binding activity.

상단으로