Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions
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 th...
| Main Authors: | , , , , , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
American Association for the Advancement of Science
2018
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| _version_ | 1797082535299121152 |
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| author | Hochberg, G Shepherd, D Marklund, E Santhanagoplan, I Degiacomi, M Laganowsky, A Allison, T Basha, E Marty, M Galpin, M Struwe, W Baldwin, A Vierling, E Benesch, J |
| author_facet | Hochberg, G Shepherd, D Marklund, E Santhanagoplan, I Degiacomi, M Laganowsky, A Allison, T Basha, E Marty, M Galpin, M Struwe, W Baldwin, A Vierling, E Benesch, J |
| author_sort | Hochberg, G |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-07T01:29:18Z |
| format | Journal article |
| id | oxford-uuid:93121a0f-46ba-4070-b6d3-05514d82363f |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T01:29:18Z |
| publishDate | 2018 |
| publisher | American Association for the Advancement of Science |
| record_format | dspace |
| spelling | oxford-uuid:93121a0f-46ba-4070-b6d3-05514d82363f2022-03-26T23:29:45ZStructural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functionsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:93121a0f-46ba-4070-b6d3-05514d82363fEnglishSymplectic Elements at OxfordAmerican Association for the Advancement of Science2018Hochberg, GShepherd, DMarklund, ESanthanagoplan, IDegiacomi, MLaganowsky, AAllison, TBasha, EMarty, MGalpin, MStruwe, WBaldwin, AVierling, EBenesch, JOligomeric 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. |
| spellingShingle | Hochberg, G Shepherd, D Marklund, E Santhanagoplan, I Degiacomi, M Laganowsky, A Allison, T Basha, E Marty, M Galpin, M Struwe, W Baldwin, A Vierling, E Benesch, J Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions |
| title | Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions |
| title_full | Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions |
| title_fullStr | Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions |
| title_full_unstemmed | Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions |
| title_short | Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions |
| title_sort | structural principles that enable oligomeric small heat shock protein paralogs to evolve distinct functions |
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