Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 25, Issue 3, Pages 279-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41594-018-0029-5
Keywords
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Funding
- ISEF foundation
- Medical Research Council [MCU105185859, MR/N020413/1]
- Boehringer Ingelheim Fond
- 'Lendulet' Programme of the Hungarian Academy of Sciences
- Wellcome Trust
- Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences
- NKFI [120220]
- National Brain Research Programme
- TEKES Finland Distinguished Professor Grant
- Ministry of Education, Culture, Sports, Science and Technology (ME5a-c)
- JSPS KAKENHI [JP17H06351]
- MEXT
- Hirao Taro Foundation of KONAN GAKUEN for Academic Research
- MRC Career Development Award [MR/M02122X/1]
- EMBO [ALTF 698-2012]
- Directorate-General for Research and Innovation (FP7-PEOPLE-2010-IEF) [ThPLAST 274192]
- EMBL Interdisciplinary Postdoctoral fellowship - H2020 Marie Sklodowska Curie Actions
- National Institutes of Health [R01 GM099865]
- [GINOP-2.3.2-15-2016-00001]
- [GINOP-2.3.2-15-2016-00026]
- MRC [MC_U105185859, MR/M02122X/1] Funding Source: UKRI
- Medical Research Council [MC_U105185859, MR/M02122X/1] Funding Source: researchfish
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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 coil 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.
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