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DOI | 10.1126/science.aam7229 |
Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions | |
Hochberg, Georg K. A.1,3; Shepherd, Dale A.1,4; Marklund, Erik G.1,5; Santhanagoplan, Indu2,6; Degiacomi, Matteo T.1,7; Laganowsky, Arthur1,8,9,10; Allison, Timothy M.1; Basha, Eman2,11; Marty, Michael T.1,11; Galpin, Martin R.1; Struwe, Weston B.1; Baldwin, Andrew J.1; Vierling, Elizabeth2; Benesch, Justin L. P.1 | |
2018-02-23 | |
发表期刊 | SCIENCE
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ISSN | 0036-8075 |
EISSN | 1095-9203 |
出版年 | 2018 |
卷号 | 359期号:6378页码:930-934 |
文章类型 | Article |
语种 | 英语 |
国家 | England; USA; Sweden |
英文摘要 | Oligomeric proteins assemble with exceptional selectivity, even in the presence of closely related proteins, to perform their cellular roles. We show that most proteins related by gene duplication of an oligomeric ancestor have evolved to avoid hetero-oligomerization and that this correlates with their acquisition of distinct functions. We report how coassembly is avoided by two oligomeric small heat-shock protein paralogs. A hierarchy of assembly, involving intermediates that are populated only fleetingly at equilibrium, ensures selective oligomerization. Conformational flexibility at noninterfacial regions in the monomers prevents coassembly, allowing interfaces to remain largely conserved. Homomeric oligomers must overcome the entropic benefit of coassembly and, accordingly, homomeric paralogs comprise fewer subunits than homomers that have no paralogs. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000425752600048 |
WOS关键词 | GENE DUPLICATION ; EVOLUTION ; STRESS ; EXPRESSION ; COMPLEXES |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
URL | 查看原文 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/198050 |
专题 | 地球科学 资源环境科学 气候变化 |
作者单位 | 1.Univ Oxford, Dept Chem, Phys & Theoret Chem Lab, Oxford OX1 3QZ, England; 2.Univ Massachusetts, Dept Biochem & Mol Biol, Amherst, MA 01003 USA; 3.Univ Chicago, Dept Ecol & Evolut, Chicago, IL 60637 USA; 4.Waters Corp, Stamford Ave, Wilmslow SK9 4AX, Cheshire, England; 5.Uppsala Univ, Dept Chem BMC, Box 576, S-75123 Uppsala, Sweden; 6.Univ Cambridge, Dept Plant Sci, Cambridge CB2 3EA, England; 7.Univ Durham, Dept Chem, South Rd, Durham DH1 3LE, England; 8.Texas A&M Hlth Sci Ctr, Inst Biosci & Technol, Ctr Infect & Inflammatory Dis, Houston, TX 77030 USA; 9.Texas A&M Univ, Dept Chem, College Stn, TX 77842 USA; 10.Texas A&M Hlth Sci Ctr, Dept Microbial Pathogenesis & Immunol, Coll Med, Bryan, TX 77807 USA; 11.Univ Arizona, Dept Chem & Biochem, 1306 East Univ Blvd, Tucson, AZ 85721 USA |
推荐引用方式 GB/T 7714 | Hochberg, Georg K. A.,Shepherd, Dale A.,Marklund, Erik G.,et al. Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions[J]. SCIENCE,2018,359(6378):930-934. |
APA | Hochberg, Georg K. A..,Shepherd, Dale A..,Marklund, Erik G..,Santhanagoplan, Indu.,Degiacomi, Matteo T..,...&Benesch, Justin L. P..(2018).Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions.SCIENCE,359(6378),930-934. |
MLA | Hochberg, Georg K. A.,et al."Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions".SCIENCE 359.6378(2018):930-934. |
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