Journal article
Unfolded protein responses in bacteria and mitochondria: A central role for the ClpXP machine
KN Truscott, A Bezawork-Geleta, DA Dougan
IUBMB Life | WILEY | Published : 2011
DOI: 10.1002/iub.526
Abstract
In the crowded environment of a cell, the protein quality control machinery, such as molecular chaperones and proteases, maintains a population of folded and hence functional proteins. The accumulation of unfolded proteins in a cell is particularly harmful as it not only reduces the concentration of active proteins but also overburdens the protein quality control machinery, which in turn, can lead to a significant increase in nonproductive folding and protein aggregation. To circumvent this problem, cells use heat shock and unfolded protein stress response pathways, which essentially sense the change to protein homeostasis upregulating protein quality control factors that act to restore the ..
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Funding Acknowledgements
KNT is supported by an Australian Research Council (ARC) Future Fellowship and DAD is supported by an ARC Australian Research Fellowship. AB-G is supported by a La Trobe University Postgraduate Research Scholarship and Fee Remission Research Scholarship. Work in this laboratory is funded by the ARC.