ArticleProtein science : a publication of the Protein Society2010
Versatile modes of peptide recognition by the ClpX N domain mediate alternative adaptor-binding specificities in different bacterial species.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- An open axial channel of the AAA ClpXP protease enhances degradation of specific classes of protein substrates.Protein science : a publication of the Protein Society · 2026Article
- ATP hydrolysis tunes specificity of a AAA+ protease.Cell reports · 2022Article
- Applications of Bacterial Degrons and Degraders - Toward Targeted Protein Degradation in Bacteria.Frontiers in molecular biosciences · 2021Review
- Protease-deficient SOS constitutive cells have RecN-dependent cell division phenotypes.Molecular microbiology · 2019Article
- Protease regulation and capacity during Caulobacter growth.Current opinion in microbiology · 2016Review
- Regulated Proteolysis in Bacteria: Caulobacter.Annual review of genetics · 2016Review
- Deciphering the Roles of Multicomponent Recognition Signals by the AAA+ Unfoldase ClpX.Journal of molecular biology · 2015Article
- A queueing approach to multi-site enzyme kinetics.Interface focus · 2014Article
- Roles of adaptor proteins in regulation of bacterial proteolysis.Current opinion in microbiology · 2013Review
- Adaptor-dependent degradation of a cell-cycle regulator uses a unique substrate architecture.Structure (London, England : 1993) · 2012Article
- Geobacillus thermodenitrificans YjbH recognizes the C-terminal end of Bacillus subtilis Spx to accelerate Spx proteolysis by ClpXP.Microbiology (Reading, England) · 2012Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
ClpXP, an AAA+ protease, plays key roles in protein-quality control and many regulatory processes in bacteria. The N-terminal domain of the ClpX component of ClpXP is involved in recognition of many protein substrates, either directly or by binding the SspB adaptor protein, which delivers specific classes of substrates for degradation. Despite very limited sequence homology between the E. coli and C. crescentus SspB orthologs, each of these adaptors can deliver substrates to the ClpXP enzyme from the other bacterial species. We show that the ClpX N domain recognizes different sequence determinants in the ClpX-binding (XB) peptides of C. crescentus SspBalpha and E. coli SspB. The C. crescentus XB determinants span 10 residues and involve interactions with multiple side chains, whereas the E. coli XB determinants span half as many residues with only a few important side chain contacts. These results demonstrate that the N domain of ClpX functions as a highly versatile platform for peptide recognition, allowing the emergence during evolution of alternative adaptor-binding specificities. Our results also reveal highly conserved residues in the XB peptides of both E. coli SspB and C. crescentus SspBalpha that play no detectable role in ClpX-binding or substrate delivery.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.