Cotranslational protein assembly imposes evolutionary constraints on homomeric proteins

Natan, Eviatar and Endoh, Endoh and Haim-Vilmovsky, Liora and Flock, Tilman and Chalancon, Guilhem and Hopper, Jonathan and Kintses, Bálint and Horváth, Péter and Daruka, Lejla and Fekete, Gergely and Pál, Csaba and Papp, Balázs and Őszi, Erika and Magyar, Zoltán (2018) Cotranslational protein assembly imposes evolutionary constraints on homomeric proteins. Nature Structural and Molecular Biology, 25. pp. 279-288. ISSN 1545-9993, ESSN: 1545-9985

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Abstract

Cotranslational protein folding can facilitate rapid formation of functional structures. However, it can 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 toward the C termini of polypeptide chains across diverse proteomes. We hypothesize that this is the result of evolutionary constraints for folding to occur before assembly. Using high-throughput imaging of protein homomers in Escherichia coli and engineered protein constructs with N- and C-terminal oligomerization domains, we show that, indeed, proteins with C-terminal homomeric interface residues consistently assemble more efficiently than those with N-terminal interface residues. Using in vivo, in vitro and in silico experiments, we identify features that govern successful assembly of homomers, which have implications for protein design and expression optimization

Item Type:	Article
Subjects:	Q Science / természettudomány > Q1 Science (General) / természettudomány általában
Depositing User:	Dr Balint Kintses
Date Deposited:	26 Sep 2018 10:27
Last Modified:	31 Jan 2019 14:37
URI:	http://real.mtak.hu/id/eprint/85337

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• Cotranslational protein assembly imposes evolutionary constraints on homomeric proteins. (deposited 26 Sep 2018 08:03)
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