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학술발표회초록보기

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  • 09월 06일 11시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제112회 대한화학회 학술발표회, 총회 및 기기전시회 안내 How does iron coordination affect the function of zinc finger proteins?

등록일
2013년 9월 3일 14시 00분 11초
접수번호
1287
발표코드
INOR1-3 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 10시 : 00분
발표형식
심포지엄
발표분야
무기화학 - Symposium for Young Inorganic Chemists
저자 및
공동저자
이승재
전북대학교 화학과 , Korea
Zinc finger proteins use zinc as a structural co-factor to function, typically by binding to nucleic acids with sequence specificity. Although zinc is typically thought to be the physiologically relevant metal ion for zinc finger protein function there is evidence that other metal ions, including iron, may replace zinc under certain conditions. Studies on iron binding to two zinc finger proteins, Tristetraprolin (TTP) and ZIF-268 will be presented. TTP has two zinc binding domains each of which is composed of three cysteine residues and one histidine residue (Cys3His) that bind zinc. TTP is an RNA binding protein that regulates inflammatory response. Peptides corresponding to the zinc binding domains were prepared and their metal binding and RNA binding properties in the presence of iron were determined using a combination of UV-visible spectroscopy and Fluorescence Anisotropy. These studies demonstrated that both ferric and ferrous iron can substitute for zinc in TTP and still remain functional: i.e. bind to RNA with sequence selectivity and specificity. We then developed a spectroscopic assay to measure the oxidative susceptibility of the iron substituted TTP peptides and determined that iron substitution increases the rate of oxidation of the peptides compared to zinc. ZIF-268 is a classical zinc finger protein that contains three zinc-binding domains of the form Cys2His2. A peptide corresponding to the zinc-binding domain of ZIF-268 was prepared and its metal and DNA binding properties determined. As with TTP, iron can substitute for zinc in ZIF-268 and the protein retains functional. These results as well as studies on the oxidative susceptibility of iron substituted ZIF-268 will be presented.

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