- 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-...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Accepted manuscript
- Files:
-
-
(pdf, 877.6KB)
-
(zip, 280.0KB)
-
- Publisher copy:
- 10.1038/s41594-018-0029-5
-
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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:
- 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
Journal article
Cotranslational protein assembly imposes evolutionary constraints on homomeric proteins.
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Boehringer Ingelheim Fond
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Hungarian Academy of Sciences
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Wellcome Trust
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