Identification of a potential hydrophobic peptide binding site in the c-terminal arm of trigger factor
文献类型：期刊论文
| 作者 | Shi, Yi; Fan, Dong-Jie; Li, Shu-Xin; Zhang, Hong-Jie; Perrett, Sarah; Zhou, Jun-Mei |
| 刊名 | Protein science
 |
| 出版日期 | 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 |
| WOS记录号 | WOS:000246727100015 |
| 出版者 | COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT |
| URI标识 | http://www.irgrid.ac.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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来源：中国科学院大学
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