tRNA concentration fine tunes protein solubility.

Abstract:

:Clusters of codons pairing to low-abundance tRNAs synchronize the translation with co-translational folding of single domains in multidomain proteins. Although proven with some examples, the impact of the ribosomal speed on the folding and solubility on a global, cell-wide level remains elusive. Here we show that upregulation of three low-abundance tRNAs in Escherichia coli increased the aggregation propensity of several cellular proteins as a result of an accelerated elongation rate. Intriguingly, alterations in the concentration of the natural tRNA pool compromised the solubility of various chaperones consequently rendering the solubility of some chaperone-dependent proteins.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Fedyunin I,Lehnhardt L,Böhmer N,Kaufmann P,Zhang G,Ignatova Z

doi

10.1016/j.febslet.2012.07.012

subject

Has Abstract

pub_date

2012-09-21 00:00:00

pages

3336-40

issue

19

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(12)00580-7

journal_volume

586

pub_type

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