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Article

Altered specificity of a AAA+ protease.

Molecular cell - 12 Jan 2007

Farrell Christopher M, Baker Tania A, Sauer Robert T

Abstract excerpt

ClpXP, an ATP-dependent protease, degrades hundreds of different intracellular proteins. ClpX chooses substrates by binding peptide tags, typically displayed at the N or C terminus of the protein to be degraded. Here, we identify a ClpX mutant that displays a 300-fold change in substrate specificity, resulting in decreased degradation of ssrA-tagged substrates but improved degradation of proteins with other...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 17218279
DOI: 10.1016/j.molcel.2006.11.018
PMCID: PMC1847774

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

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Altered specificity of a AAA+ protease.PMID 17218279Read ↗

Substrate recognition and processing by a Walker B mutant of the human mitochondrial AAA+ protein CLPX.Semantic proximity Read ↗

Conserved residues in the N-domain of the AAA+ chaperone ClpA regulate substrate recognition and unfolding.Semantic proximity Read ↗

Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysisSemantic proximity Read ↗

The Intrinsically Disordered N-terminal Extension of the ClpS Adaptor Reprograms Its Partner AAA+ ClpAP Protease.Semantic proximity Read ↗

C-terminal domain mutations in ClpX uncouple substrate binding from an engagement step required for unfolding.Semantic proximity Read ↗

Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding.Semantic proximity Read ↗

A conformational switch underlies ClpP protease function.Semantic proximity Read ↗

A mitochondrial insertion directs substrate selection and engagement by ClpXSemantic proximity Read ↗

Flexible linkers leash the substrate binding domain of SspB to a peptide module that stabilizes delivery complexes with the AAA+ ClpXP protease.Semantic proximity Read ↗

Distinct static and dynamic interactions control ATPase-peptidase communication in a AAA+ protease.Semantic proximity Read ↗

Dynamic and static components power unfolding in topologically closed rings of a AAA+ proteolytic machine.Semantic proximity Read ↗

AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control.Semantic proximity Read ↗

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