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Minimum-noise production of translation factor eIF4G maps to a mechanistically determined optimal rate control window for protein synthesis

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Meng, Xiang, Firczuk, Helena, Pietroni, Paola, Westbrook, Richard, Dacheux, Estelle, Mendes, Pedro and McCarthy, John E. G. (2016) Minimum-noise production of translation factor eIF4G maps to a mechanistically determined optimal rate control window for protein synthesis. Nucleic Acids Research, 45 (2). pp. 1015-1025. doi:10.1093/nar/gkw1194

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Official URL: http://dx.doi.org/10.1093/nar/gkw1194

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Abstract

Gene expression noise influences organism evolution and fitness. The mechanisms determining the relationship between stochasticity and the functional role of translation machinery components are critical to viability. eIF4G is an essential translation factor that exerts strong control over protein synthesis. We observe an asymmetric, approximately bell-shaped, relationship between the average intracellular abundance of eIF4G and rates of cell population growth and global mRNA translation, with peak rates occurring at normal physiological abundance. This relationship fits a computational model in which eIF4G is at the core of a multi-component– complex assembly pathway. This model also correctly predicts a plateau-like response of translation to super-physiological increases in abundance of the other cap-complex factors, eIF4E and eIF4A. Engineered changes in eIF4G abundance amplify noise, demonstrating that minimum stochasticity coincides with physiological abundance of this factor. Noise is not increased when eIF4E is overproduced. Plasmid-mediated synthesis of eIF4G imposes increased global gene expression stochasticity and reduced viability because the intrinsic noise for this factor influences total cellular gene noise. The naturally evolved eIF4G gene expression noise minimum maps within the optimal activity zone dictated by eIF4G’s mechanistic role. Rate control and noise are therefore interdependent and have co-evolved to share an optimal physiological abundance point.

Item Type: Journal Article
Subjects: Q Science > QP Physiology
T Technology > TP Chemical technology
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Proteins -- Synthesis, Protein engineering, Messenger RNA, Physiology -- Research
Journal or Publication Title: Nucleic Acids Research
Publisher: Oxford University Press
ISSN: 0305-1048
Official Date: 7 December 2016
Dates:
DateEvent
7 December 2016Published
17 November 2016Accepted
24 October 2016Submitted
Volume: 45
Number: 2
Page Range: pp. 1015-1025
DOI: 10.1093/nar/gkw1194
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access
Funder: Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), National Institute of General Medical Sciences (U.S.) (NIGMS), National Institutes of Health (U.S.) (NIH)
Grant number: BB/1008349/1, BB/1020535/1, BB/M017982/1 (BBSRC), GM080219 (NIH) (NIGMS)
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