Chance, destiny, and the inner workings of ClpXP

Rick Russell; Andreas Matouschek

doi:10.1016/j.cell.2014.07.009

Chance, destiny, and the inner workings of ClpXP

Cell. 2014 Jul 31;158(3):479-80. doi: 10.1016/j.cell.2014.07.009.

Authors

Rick Russell¹, Andreas Matouschek²

Affiliations

¹ Department of Molecular Biosciences and the Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA. Electronic address: rick_russell@cm.utexas.edu.
² Department of Molecular Biosciences and the Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA. Electronic address: matouschek@austin.utexas.edu.

Abstract

AAA+ proteases are responsible for protein degradation in all branches of life. Using single-molecule and ensemble assays, Cordova et al. investigate how the bacterial protease ClpXP steps through a substrate's polypeptide chain and construct a quantitative kinetic model that recapitulates the interplay between stochastic and deterministic behaviors of ClpXP.

Publication types

Comment

MeSH terms

Endopeptidase Clp / chemistry*
Endopeptidase Clp / metabolism*

Substances

ClpP protein, human
Endopeptidase Clp
CLPX protein, human

Abstract

Publication types

MeSH terms

Substances

Grant support