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Slowing bacterial translation speed enhances eukaryotic protein folding efficiency.

Abstract：

:The mechanisms for de novo protein folding differ significantly between bacteria and eukaryotes, as evidenced by the often observed poor yields of native eukaryotic proteins upon recombinant production in bacterial systems. Polypeptide synthesis rates are faster in bacteria than in eukaryotes, but the effects of general variations in translation rates on protein folding efficiency have remained largely unexplored. By employing Escherichia coli cells with mutant ribosomes whose translation speed can be modulated, we show here that reducing polypeptide elongation rates leads to enhanced folding of diverse proteins of eukaryotic origin. These results suggest that in eukaryotes, protein folding necessitates slow translation rates. In contrast, folding in bacteria appears to be uncoupled from protein synthesis, explaining our findings that a generalized reduction in translation speed does not adversely impact the folding of the endogenous bacterial proteome. Utilization of this strategy has allowed the production of a native eukaryotic multidomain protein that has been previously unattainable in bacterial systems and may constitute a general alternative to the production of aggregation-prone recombinant proteins.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Siller E,DeZwaan DC,Anderson JF,Freeman BC,Barral JM

doi

10.1016/j.jmb.2009.12.042

subject

Has Abstract

pub_date

2010-03-12 00:00:00

pages

1310-8

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(09)01549-6

journal_volume

396

pub_type

杂志文章

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