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Journal article

Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions

Abstract:

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 o...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1126/science.aam7229

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Role:
Author
ORCID:
0000-0002-7155-0451
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Role:
Author
ORCID:
0000-0001-9301-1777
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Role:
Author
ORCID:
0000-0002-9804-5009
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Role:
Author
ORCID:
0000-0002-3039-8123
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Role:
Author
ORCID:
0000-0003-4672-471X
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Name:
Biotechnology and Biological Sciences Research Council
Grant:
BB/K004247/1
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Name:
Engineering and Physical Sciences Research Council
Grant:
EP/J01835X/1
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Name:
Royal Society
Grant:
J.L.P.B. for a University Research Fellowship
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Name:
National Institutes of Health
Grant:
R01 GM027616
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Name:
Swiss National Science Foundation
Publisher:
American Association for the Advancement of Science
Journal:
Science More from this journal
Volume:
359
Issue:
6378
Pages:
930-935
Publication date:
2018-02-23
Acceptance date:
2018-01-08
DOI:
EISSN:
1095-9203
ISSN:
0036-8075
Language:
English
Pubs id:
pubs:827320
UUID:
uuid:93121a0f-46ba-4070-b6d3-05514d82363f
Local pid:
pubs:827320
Source identifiers:
827320
Deposit date:
2018-03-03

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