The c-terminal (331-376) sequence of Escherichia coli DnaJ is essential for dimerization and chaperone activity - A small angle x-ray scattering study in solution
Shi, YY; Hong XG(洪新国); Hong, XG; Wang, CC
刊名JOURNAL OF BIOLOGICAL CHEMISTRY
2005
卷号280期号:24页码:22761-22768
学科分类Biochemistry & Molecular Biology
DOI10.1074/jbc.M503643200
通讯作者Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China ; Chinese Acad Sci, Inst High Energy Phys, Beijing 100039, Peoples R China ; Chinese Acad Sci, Grad Sch, Beijing, Peoples R China
文章类型Article
英文摘要DnaJ, an Escherichia coli Hsp40 protein composed of 376 amino acid residues, is a chaperone with thioldisulfide oxidoreductase activity. We present here for the first time a small angle x-ray scattering study of intact DnaJ and a truncated version, DnaJ (1-330), in solution. The molecular weight of DnaJ and DnaJ (1-330) determined by both small angle x-ray scattering and size-exclusion chromatography provide direct evidence that DnaJ is a homodimer and DnaJ (1-330) is a monomer. The restored models show that DnaJ is a distorted omega-shaped dimeric molecule with the C terminus of each subunit forming the central part of the omega, whereas DnaJ (1-330) exists as a monomer. This indicates that the deletion of the C-terminal 46 residues of DnaJ impairs the association sites, although it does not cause significant conformational changes. Biochemical studies reveal that DnaJ (1-330), while fully retaining its thiol-disulfide oxidoreductase activity, is structurally less stable, and its peptide binding capacity is severely impaired relative to that of the intact molecule. Together, our results reveal that the C-terminal (331-376) residues are directly involved in dimerization, and the dimeric structure of DnaJ is necessary for its chaperone activity but not required for the thiol-disulfide oxidoreductase activity.
类目[WOS]Biochemistry & Molecular Biology
研究领域[WOS]Biochemistry & Molecular Biology
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语种英语
WOS记录号WOS:000229741800026
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被引频次:35[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ihep.ac.cn/handle/311005/240203
专题中国科学院高能物理研究所_多学科研究中心_期刊论文
作者单位中国科学院高能物理研究所
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Shi, YY,Hong XG,Hong, XG,et al. The c-terminal (331-376) sequence of Escherichia coli DnaJ is essential for dimerization and chaperone activity - A small angle x-ray scattering study in solution[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2005,280(24):22761-22768.
APA Shi, YY,洪新国,Hong, XG,&Wang, CC.(2005).The c-terminal (331-376) sequence of Escherichia coli DnaJ is essential for dimerization and chaperone activity - A small angle x-ray scattering study in solution.JOURNAL OF BIOLOGICAL CHEMISTRY,280(24),22761-22768.
MLA Shi, YY,et al."The c-terminal (331-376) sequence of Escherichia coli DnaJ is essential for dimerization and chaperone activity - A small angle x-ray scattering study in solution".JOURNAL OF BIOLOGICAL CHEMISTRY 280.24(2005):22761-22768.
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