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Mechanically Watching the ClpXP Proteolytic Machinery
2016Energy-dependent protein degradation is studied through the dual bead ClpXP motility assay. Processing of folded proteins involves recognition, unfolding, translocation, and degradation stages. A dual optical trap, in a passive force-clamp geometry, exhibits bead-to-bead displacements that directly follow subprocesses underlying protein degradation ...
Juan Carlos, Cordova +2 more
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Unfolding and Translocation of Proteins Through an Alpha-Hemolysin Nanopore by ClpXP
2020Proteins present a significant challenge for nanopore-based sequence analysis. This is partly due to their stable tertiary structures that must be unfolded for linear translocation, and the absence of regular charge density. To address these challenges, here we describe how ClpXP, an ATP-dependent protein unfoldase, can be harnessed to unfold and ...
Jeff, Nivala +4 more
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An adaptor for feedback regulation of heme biosynthesis by the mitochondrial protease CLPXP
ABSTRACT Heme biosynthesis is tightly coordinated such that essential heme functions including oxygen transport, respiration, and catalysis are fully supplied without overproducing toxic heme precursors and depleting cellular iron. The initial heme biosynthetic enzyme, ALA synthase (ALAS), exhibits heme-induced degradation that is ...Thomas Cottle +4 more
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ATP-dependent protein degradation and unfolding by ClpXP
GBM Annual Fall meeting Halle 2002, 2002R.T. Sauer +9 more
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Strain-Dependent Recognition of a Unique Degradation Motif by ClpXP in Streptococcus mutans.
MSphere, 2016Indranil Biswas, Liang Tao
exaly