The minimal alpha-crystallin domain of Mj Hsp 16.5 is functional at non-heat-shock conditions
文献类型：期刊论文
| 作者 | Xi, Dong1,2; Wei, Ping2; Zhang, Changsheng1; Lai, Luhua1,2 |
| 刊名 | PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
 |
| 出版日期 | 2014-07-01 |
| 卷号 | 82期号:7页码:1156-1167 |
| 关键词 | Mj Hsp16.5 Small Heat Shock Protein Alpha-crystallin Domain Beta-strand Exchange Loop Chaperone-like Activity Protein Aggregation Mechanism |
| ISSN号 | 0887-3585 |
| DOI | 10.1002/prot.24480 |
| 英文摘要 | The small heat shock protein (sHSP) from Methanococcus jannaschii (Mj Hsp16.5) forms a monodisperse 24mer and each of its monomer contains two flexible N- and C-terminals and a rigid -crystallin domain with an extruding -strand exchange loop. The minimal -crystallin domain with a -sandwich fold is conserved in sHSP family, while the presence of the -strand exchange loop is divergent. The function of the -strand exchange loop and the minimal -crystallin domain of Mj Hsp16.5 need further study. In the present study, we constructed two fragment-deletion mutants of Mj Hsp16.5, one with both the N- and C-terminals deleted (NC) and the other with a further deletion of the -strand exchange loop (NLC). NC existed as a dimer in solution. In contrast, the minimal -crystallin domain NLC became polydisperse in solution and exhibited more efficient chaperone-like activities to prevent amorphous aggregation of insulin B chain and fibril formation of the amyloidogenic peptide dansyl-SSTSAA-W than the mutant NC and the wild type did. The hydrophobic probe binding experiments indicated that NLC exposed much more hydrophobic surface than NC. Our study also demonstrated that Mj Hsp16.5 used different mechanisms for protecting different substrates. Though Mj Hsp16.5 formed stable complexes with substrates when preventing thermal aggregation, no complexes were detected when preventing aggregation under non-heat-shock conditions. Proteins 2014; 82:1156-1167. (c) 2013 Wiley Periodicals, Inc. |
| 语种 | 英语 |
| WOS记录号 | WOS:000337474700005 |
| 出版者 | WILEY-BLACKWELL |
| 源URL | [http://ir.iccas.ac.cn/handle/121111/50031]  |
| 专题 | 中国科学院化学研究所 |
| 通讯作者 | Lai, Luhua |
| 作者单位 | 1.Peking Univ, Coll Chem & Mol Engn, State Key Lab Struct Chem Unstable & Stable Speci, BNLMS, Beijing 100871, Peoples R China 2.Peking Univ, Ctr Quantitat Biol, Beijing 100871, Peoples R China |
| 推荐引用方式 GB/T 7714 | Xi, Dong,Wei, Ping,Zhang, Changsheng,et al. The minimal alpha-crystallin domain of Mj Hsp 16.5 is functional at non-heat-shock conditions[J]. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,2014,82(7):1156-1167. |
| APA | Xi, Dong,Wei, Ping,Zhang, Changsheng,&Lai, Luhua.(2014).The minimal alpha-crystallin domain of Mj Hsp 16.5 is functional at non-heat-shock conditions.PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,82(7),1156-1167. |
| MLA | Xi, Dong,et al."The minimal alpha-crystallin domain of Mj Hsp 16.5 is functional at non-heat-shock conditions".PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 82.7(2014):1156-1167. |
入库方式： OAI收割
来源：化学研究所
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