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 re

SUBMITTER: Belle A 

PROVIDER: S-EPMC1550773 | biostudies-literature | 2006 Aug

REPOSITORIES: biostudies-literature