Open AccessStructural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions
Author(s) -
Georg Hochberg,
Dale A. Shepherd,
Erik G. Marklund,
Indu Santhanagoplan,
Matteo T. Degiacomi,
Arthur Laganowsky,
Timothy M. Allison,
Eman Basha,
Michael T. Marty,
Martin R. Galpin,
Weston B. Struwe,
Andrew J. Baldwin,
Elizabeth Vierling,
Justin L. P. Benesch
Publication year - 2018
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.aam7229
Subject(s) - homomeric , biology , flexibility (engineering) , gene duplication , protocell , evolvability , heat shock protein , functional divergence , gene , biophysics , computational biology , evolutionary biology , genetics , gene family , gene expression , protein subunit , statistics , mathematics , membrane
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. Hochberget 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
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