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Cotranslational protein assembly imposes evolutionary constraints on homomeric proteins.

Abstract:

Cotranslational protein folding can facilitate rapid formation of functional structures. However, it might also cause premature assembly of protein complexes, if two interacting nascent chains are in close proximity. By analyzing known protein structures, we show that homomeric protein contacts are enriched towards the C-termini of polypeptide chains across diverse proteomes. We hypothesize that this is the result of evolutionary constraints for folding to occur prior to assembly. Using high-...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Accepted manuscript

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Publisher copy:
10.1038/s41594-018-0029-5

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Role:
Author
ORCID:
0000-0002-0323-0034
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Role:
Author
ORCID:
0000-0003-3398-0968
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Boehringer Ingelheim Fond More from this funder
Hungarian Academy of Sciences More from this funder
Wellcome Trust More from this funder
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Publisher:
Nature Publishing Group Publisher's website
Journal:
Nature Structural and Molecular Biology Journal website
Volume:
25
Issue:
3
Pages:
279-288
Publication date:
2018-02-12
Acceptance date:
2018-01-10
DOI:
EISSN:
1545-9985
ISSN:
1545-9993
Pubs id:
pubs:825592
URN:
uri:94b40742-f704-472b-8757-b2a9363555b7
UUID:
uuid:94b40742-f704-472b-8757-b2a9363555b7
Local pid:
pubs:825592
Language:
English
Keywords:

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