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

	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
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
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.
学科主题	Biochemistry & Molecular Biology
类目[WOS]	Biochemistry & Molecular Biology
研究领域[WOS]	Biochemistry & Molecular Biology
原文出处	SCI
语种	英语
WOS记录号	WOS:000229741800026
内容类型	期刊论文
源URL	[http://ir.ihep.ac.cn/handle/311005/240203]
专题	高能物理研究所_多学科研究中心
作者单位	中国科学院高能物理研究所
推荐引用方式 GB/T 7714	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.