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Vol. 12, Issue 3, 577-588, March 2001
Howard Hughes Medical Institute and Department of Biochemistry and
Biophysics, University of California, San Francisco, San Francisco,
California 94143-0448
Translational control has recently been recognized as an important
facet of adaptive responses to various stress conditions. We describe
the adaptation response of the yeast Saccharomyces cerevisiae to the loss of one of two mechanisms to target
proteins to the secretory pathway. Using inducible mutants that block
the signal recognition particle (SRP) pathway, we find that cells demonstrate a physiological response to the loss of the SRP pathway that includes specific changes in global gene expression. Upon inducing
the loss of the SRP pathway, SRP-dependent protein translocation is
initially blocked, and cell growth is considerably slowed. Concomitantly, gene expression changes include the induction of heat
shock genes and the repression of protein synthesis genes. Remarkably,
within hours, the efficiency of protein sorting improves while cell
growth remains slow in agreement with the persistent repression of
protein synthesis genes. Our results suggest that heat shock gene
induction serves to protect cells from mislocalized precursor proteins
in the cytosol, whereas reduced protein synthesis helps to regain
efficiency in protein sorting by reducing the load on the protein
translocation apparatus. Thus, we suggest that cells trade
speed in cell growth for fidelity in protein sorting to
adjust to life without SRP.
Online version of this article contains
data set material. Online version available at www.molbiolcell.org.
*
Corresponding author. E-mail address: walter{at}cgl.ucsf.edu.
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