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	Identification of a potential hydrophobic peptide binding site in the c-terminal arm of trigger factor
	Shi, Yi; Fan, Dong-Jie; Li, Shu-Xin; Zhang, Hong-Jie; Perrett, Sarah; Zhou, Jun-Mei
刊名	Protein science
	2007-06-01
卷号	16期号:6页码:1165-1175
关键词	Trigger factor Chaperone Binding site Bis-ans Hydrophobic interaction
ISSN号	0961-8368
DOI	10.1110/ps.062623707
通讯作者	Zhou, jun-mei(zhoujm@sun5.ibp.ac.cn)
英文摘要	Trigger factor (tf) is the first chaperone to interact with nascent chains and facilitate their folding in bacteria. escherichia coli tf is 432 residues in length and contains three domains with distinct structural and functional properties. the n-terminal domain of tf is important for ribosome binding, and the m-domain carries the ppiase activity. however, the function of the c-terminal domain remains unclear, and the residues or regions directly involved in substrate binding have not yet been identified. here, a hydrophobic probe, bis-ans, was used to characterize potential substrate-binding regions. results showed that bis-ans binds tf with a 1:1 stoichiometry and a k-d of 16 mu m, and it can be covalently incorporated into tf by uv-light irradiation. a single bis-ans-labeled peptide was obtained by tryptic digestion and identified by maldi-tof mass spectrometry as asn391-lys392. in silico docking analysis identified a single potential binding site for bis-ans on the tf molecule, which is adjacent to this dipeptide and lies in the pocket formed by the c-terminal arms. the bis-ans-labeled tf completely lost the ability to assist gapdh or lysozyme refolding and showed increased protection toward cleavage by alpha-chymotrypsin, suggesting blocking of hydrophobic residues. the c-terminal truncation mutant tf389 also showed no chaperone activity and could not bind bis-ans. these results suggest that bis-ans binding may mimic binding of a substrate peptide and that the c-terminal region of tf plays an important role in hydrophobic binding and chaperone function.
WOS关键词	ESCHERICHIA-COLI ; 1,1'-BI(4-ANILINO)NAPHTHALENE-5,5'-DISULFONIC ACID ; D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE ; NASCENT POLYPEPTIDES ; ISOMERASE ACTIVITY ; CHAPERONE ACTIVITY ; PROLYL ISOMERASE ; ALPHA-CRYSTALLIN ; ENERGY-TRANSFER ; APICAL DOMAIN
WOS研究方向	Biochemistry & Molecular Biology
WOS类目	Biochemistry & Molecular Biology
语种	英语
出版者	COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
WOS记录号	WOS:000246727100015
内容类型	期刊论文
URI标识	http://www.corc.org.cn/handle/1471x/2380680
专题	中国科学院大学
通讯作者	Zhou, Jun-Mei
作者单位	1.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China 2.Chinese Acad Sci, Inst Biophys, Ctr Syst Biol, Beijing 100101, Peoples R China 3.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China
推荐引用方式 GB/T 7714	Shi, Yi,Fan, Dong-Jie,Li, Shu-Xin,et al. Identification of a potential hydrophobic peptide binding site in the c-terminal arm of trigger factor[J]. Protein science,2007,16(6):1165-1175.
APA	Shi, Yi,Fan, Dong-Jie,Li, Shu-Xin,Zhang, Hong-Jie,Perrett, Sarah,&Zhou, Jun-Mei.(2007).Identification of a potential hydrophobic peptide binding site in the c-terminal arm of trigger factor.Protein science,16(6),1165-1175.
MLA	Shi, Yi,et al."Identification of a potential hydrophobic peptide binding site in the c-terminal arm of trigger factor".Protein science 16.6(2007):1165-1175.

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