Quantification of protein half-lives in the budding yeast proteome.

Abstract:

:A complete description of protein metabolism requires knowledge of the rates of protein production and destruction within cells. Using an epitope-tagged strain collection, we measured the half-life of >3,750 proteins in the yeast proteome after inhibition of translation. By integrating our data with previous measurements of protein and mRNA abundance and translation rate, we provide evidence that many proteins partition into one of two regimes for protein metabolism: one optimized for efficient production or a second optimized for regulatory efficiency. Incorporation of protein half-life information into a simple quantitative model for protein production improves our ability to predict steady-state protein abundance values. Analysis of a simple dynamic protein production model reveals a remarkable correlation between transcriptional regulation and protein half-life within some groups of coregulated genes, suggesting that cells coordinate these two processes to achieve uniform effects on protein abundances. Our experimental data and theoretical analysis underscore the importance of an integrative approach to the complex interplay between protein degradation, transcriptional regulation, and other determinants of protein metabolism.

authors

Belle A,Tanay A,Bitincka L,Shamir R,O'Shea EK

doi

10.1073/pnas.0605420103

subject

Has Abstract

pub_date

2006-08-29 00:00:00

pages

13004-9

issue

35

eissn

0027-8424

issn

1091-6490

pii

0605420103

journal_volume

103

pub_type

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