ClpXP, an ATP-powered unfolding and protein-degradation machine
Name
Baker_ClpXP an ATP.pdf
Size
2.11 MB
Format
Adobe PDF
Checksum (MD5)
b4c6e82aeea4a154e09a87121ba0c205
Author(s)
Baker, Tania
Sauer, Robert T
Date Issued
June 2011
Journal
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Publisher
Elsevier
Citation
Baker, Tania A., and Robert T. Sauer. “ClpXP, an ATP-powered unfolding and protein-degradation machine.” Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1823, no. 1 (January 2012): 15-28. Copyright © 2011 Elsevier B.V.
Version
Final published version
Abstract
ClpXP is a AAA+ protease that uses the energy of ATP binding and hydrolysis to perform mechanical work during targeted protein degradation within cells. ClpXP consists of hexamers of a AAA+ ATPase (ClpX) and a tetradecameric peptidase (ClpP). Asymmetric ClpX hexamers bind unstructured peptide tags in protein substrates, unfold stable tertiary structure in the substrate, and then translocate the unfolded polypeptide chain into an internal proteolytic compartment in ClpP. Here, we review our present understanding of ClpXP structure and function, as revealed by two decades of biochemical and biophysical studies. This article is part of a Special Issue entitled: AAA ATPases: Structure and function.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Terms of Use
Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1016/j.bbamcr.2011.06.007
