The Journal of Natural Sciences (자연과학논문집)
- Volume 17 Issue 1
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- Pages.13-29
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- 2006
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- 1225-6196(pISSN)
Characterization of the Interaction of Sulfiredoxin (Srx1) with a Vacoular Protein $\alpha$ -Mannosidase (Ams1) in Saccharomyces cerevisiae
설피리독신과 알파-만노시다제 간의 단백질 결합 특성에 관한 고찰
- Barando, Karen P. (Department of Biochemistry, Paichai University) ;
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Kim, Il-Han
(Department of Biochemistry, Paichai University)
- Published : 2006.12.29
Abstract
Most redox-active proteins have thiol-bearing cysteine residues that are sensitive to oxidation. Cysteine thiols oxidized to sulfenic acid are generally unstable, either forming a disulfide with a nearby thiol or being further oxidized to a stable sulfinic acid, which have been viewed as an irreversible protein modification. However, recent studies showed that cysteine residues of certain thiol peroxidases (Prxs) undergo reversible oxidation to sulfinic acid and the reduction reaction is catalyzed by sulfiredoxin (Srx1). Specific Cys residues of various other proteins are also oxidized to sulfinic acid (
산화-환원 활성 단백질중에 하나인 설피레독신과의 결합 단백질을 효모 Two-hybrid 기법을 이용하여 탐색한 결과, 알파-만노시다제가 설피레독신과 특이적으로 결합함을 밝혔다. 알파-만노시다제는 D-만노스 당을 비환원성 말단으로부터 유리시키는 가수분해 효소로서, 세포 원형질에 다량체 형태로 존재한다. 본 연구에서는 설피레독신과 알파-만노시다제간의 단백질결합을 설피레독신의 새로운 생리기능 관점에서 토의했다.