Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions
| Autor: | Georg K. A. Hochberg, Erik G. Marklund, Weston B. Struwe, Eman Basha, Dale A. Shepherd, Martin R. Galpin, Timothy M. Allison, Elizabeth Vierling, Matteo T. Degiacomi, Andrew Baldwin, Michael T. Marty, Indu Santhanagoplan, Justin L. P. Benesch, Arthur Laganowsky |
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| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Multidisciplinary Chemistry Extramural Protein Conformation Protein subunit Protein domain Protein multimerization Article Heat-Shock Proteins Small 03 medical and health sciences Protein Subunits 030104 developmental biology Protein structure Protein Domains Heat shock protein Gene Duplication Gene duplication Biophysics Homomeric Protein Multimerization |
| Zdroj: | Science Science, 2018, Vol.359(6378), pp.930-935 [Peer Reviewed Journal] |
| Popis: | Putting distance between protein relatives Many proteins form complexes to function. When the gene for a self-assembling protein duplicates, it might be expected that the related proteins (paralogs) would retain interfaces that would allow coassembly. Hochberg et al. show that the majority of paralogs that oligomerize in fact self-assemble. These paralogs have more diverse functions than those that coassemble, implying that maintaining coassembly would constrain evolution of new function. The authors experimentally investigated how two oligomeric small heat-shock protein paralogs avoid coassembly and found that flexibility at regions outside of the interaction interfaces played a key role. Science , this issue p. 930 |
| Databáze: | OpenAIRE |
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