Contributions of cysteine residues in zn2 to zinc fingers and thiol-disulfide oxidoreductase activities of chaperone dnaj | |
Shi, YY; Tang, W; Hao, SF; Wang, CC | |
刊名 | Biochemistry |
2005-02-08 | |
卷号 | 44期号:5页码:1683-1689 |
ISSN号 | 0006-2960 |
DOI | 10.1021/bi0480943 |
通讯作者 | Wang, cc() |
英文摘要 | Escherichia coli dnaj, possessing both chaperone and thiol-disulfide oxidoreductase activities, is a homodimeric hsp40 protein. each subunit contains four copies of a sequence of -cxxcxgxg-, which coordinate with two zn(ii) ions to form an unusual topology of two c-4-type zinc fingers, (cdvczn)-d-144-zn-147(ii)(cnkc200)-n-197 (zn1) and (cptczn)-p-161-zn-164(ii)(cphc116)-p-183(zn2). studies on five dnaj mutants with cys in zn2 replaced by his or ser (c183h, c186h, c161h/c183h, c164h/183h, and c161s/ c164s) reveal that substitutions of one or two cys residues by his or ser have little effect on the general conformation and association property of the molecule. replacement of two cys residues by his does not interfere with the zinc coordination. however, replacement of two cys by ser results in a significant decrease in the proportion of coordinated zn(ii), although the unique zinc finger topology is retained. the mutants of c183h, c186h, and c161s/c164s display full disulfide reductase activity of wild-type dnaj, while c 161 h/c183h and c164h/183h exhibit severe defect in the activity. all of the mutations do not substantially affect the chaperone activity. the results indicate that the motif of -cxxc- is critical to form an active site and indispensable to the thiol-disulfide oxidoreductase activity of dnaj. each -cxxc- motif in zn2 but not in zn1 functions as an active site. |
WOS关键词 | ESCHERICHIA-COLI ; NUCLEOCAPSID PROTEIN ; BINDING ; THIOREDOXIN ; ISOMERASE ; PURIFICATION ; DISSOCIATION ; REDUCTION ; DOMAIN ; SITES |
WOS研究方向 | Biochemistry & Molecular Biology |
WOS类目 | Biochemistry & Molecular Biology |
语种 | 英语 |
出版者 | AMER CHEMICAL SOC |
WOS记录号 | WOS:000226802000031 |
内容类型 | 期刊论文 |
URI标识 | http://www.corc.org.cn/handle/1471x/2378338 |
专题 | 中国科学院大学 |
通讯作者 | Wang, CC |
作者单位 | 1.Chinese Acad Sci, Inst Biophys, Natl Biomacromol, Beijing 100101, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100101, Peoples R China |
推荐引用方式 GB/T 7714 | Shi, YY,Tang, W,Hao, SF,et al. Contributions of cysteine residues in zn2 to zinc fingers and thiol-disulfide oxidoreductase activities of chaperone dnaj[J]. Biochemistry,2005,44(5):1683-1689. |
APA | Shi, YY,Tang, W,Hao, SF,&Wang, CC.(2005).Contributions of cysteine residues in zn2 to zinc fingers and thiol-disulfide oxidoreductase activities of chaperone dnaj.Biochemistry,44(5),1683-1689. |
MLA | Shi, YY,et al."Contributions of cysteine residues in zn2 to zinc fingers and thiol-disulfide oxidoreductase activities of chaperone dnaj".Biochemistry 44.5(2005):1683-1689. |
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