Journal article
Cotranslational protein assembly imposes evolutionary constraints on homomeric proteins.
- Abstract:
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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
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- Files:
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(Accepted manuscript, pdf, 877.6KB)
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(Accepted manuscript, zip, 280.0KB)
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- Publisher copy:
- 10.1038/s41594-018-0029-5
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Authors
Funding
Hungarian Academy of Sciences
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Boehringer Ingelheim Fond
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Wellcome Trust
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Bibliographic Details
- 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:
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1545-9985
- ISSN:
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1545-9993
- Pmid:
-
29434345
- Source identifiers:
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825592
Item Description
- Language:
- English
- Keywords:
- Pubs id:
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pubs:825592
- UUID:
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uuid:94b40742-f704-472b-8757-b2a9363555b7
- Local pid:
- pubs:825592
- Deposit date:
- 2018-06-11
Terms of use
- Copyright holder:
- Nature America Inc
- Copyright date:
- 2018
- Notes:
- © 2018 Nature America Inc., part of Springer Nature. All rights reserved.This is the accepted manuscript version of the article. The final version is available online from Nature Publishing Group at: https://doi.org/10.1038/s41594-018-0029-5
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