Transient ribosomal attenuation coordinates protein synthesis and co-translational folding.

Abstract:

:Clustered codons that pair to low-abundance tRNA isoacceptors can form slow-translating regions in the mRNA and cause transient ribosomal arrest. We report that folding efficiency of the Escherichia coli multidomain protein SufI can be severely perturbed by alterations in ribosome-mediated translational attenuation. Such alterations were achieved by global acceleration of the translation rate with tRNA excess in vitro or by synonymous substitutions to codons with highly abundant tRNAs both in vitro and in vivo. Conversely, the global slow-down of the translation rate modulated by low temperature suppresses the deleterious effect of the altered translational attenuation pattern. We propose that local discontinuous translation temporally separates the translation of segments of the peptide chain and actively coordinates their co-translational folding.

journal_name

Nat Struct Mol Biol

authors

Zhang G,Hubalewska M,Ignatova Z

doi

10.1038/nsmb.1554

subject

Has Abstract

pub_date

2009-03-01 00:00:00

pages

274-80

issue

3

eissn

1545-9993

issn

1545-9985

pii

nsmb.1554

journal_volume

16

pub_type

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