ArticleJournal of molecular biology2013
E. coli ClpA catalyzed polypeptide translocation is allosterically controlled by the protease ClpP.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 48 citations in OpenAlex.
- ClpA- and ClpAP-catalyzed unfolding and translocation are differentially coupled to ATP binding.Biophysical journal · 2026Article
- Linked dimers of the AAA+ ATPase Msp1 reveal energetic demands and mechanistic plasticity for substrate extraction from lipid bilayers.FEBS letters · 2026Article
- Structure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP.Communications biology · 2025Article
- Single turnover transient state kinetics reveals processive protein unfolding catalyzed byeLife · 2024Article
- Lon degrades stable substrates slowly but with enhanced processivity, redefining the attributes of a successful AAA+ protease.Cell reports · 2023Article
- Uncovering the mechanisms of transcription elongation by eukaryotic RNA polymerases I, II, and III.iScience · 2022Article
- The activated ClpP peptidase forcefully grips a protein substrate.Biophysical journal · 2022Article
- AAA+ proteins: one motor, multiple ways to work.Biochemical Society transactions · 2022Review
- Multi-start Evolutionary Nonlinear OpTimizeR (MENOTR): A hybrid parameter optimization toolbox.Biophysical chemistry · 2021Article
- Herding cats: Label-based approaches in protein translocation through nanopore sensors for single-molecule protein sequence analysis.iScience · 2021Review
- Transcriptome analysis of Escherichia coli K1 after therapy with hesperidin conjugated with silver nanoparticles.BMC microbiology · 2021Article
- The Cleavage Profile of Protein Substrates by ClpXP Reveals Deliberate Starts and Pauses.Biochemistry · 2020Article
- Kinetic Analysis of AAA+ Translocases by Combined Fluorescence and Anisotropy Methods.Biophysical journal · 2020Article
- Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis.Nature structural & molecular biology · 2020Article
- Synonymous codon substitutions perturb cotranslational protein folding in vivo and impair cell fitness.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Examination of the nucleotide-linked assembly mechanism of E. coli ClpA.Protein science : a publication of the Protein Society · 2019Article
- Hsp104 and Potentiated Variants Can Operate as Distinct Nonprocessive Translocases.Biophysical journal · 2019Article
- A High-Throughput Interbacterial Competition Screen Identifies ClpAP in Enhancing Recipient Susceptibility to Type VI Secretion System-Mediated Attack byFrontiers in microbiology · 2019Article
- Cotranslocational processing of the protein substrate calmodulin by an AAA+ unfoldase occurs via unfolding and refolding intermediates.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Comparative roles of clpA and clpB in the survival of S. Typhimurium under stress and virulence in poultry.Scientific reports · 2018Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
There are five known ATP-dependent proteases in Escherichia coli (Lon, ClpAP, ClpXP, HslUV, and the membrane-associated FtsH) that catalyze the removal of both misfolded and properly folded proteins in cellular protein quality control pathways. Hexameric ClpA rings associate with one or both faces of the cylindrically shaped tetradecameric ClpP protease. ClpA catalyzes unfolding and translocation of polypeptide substrates into the proteolytic core of ClpP for degradation through repeated cycles of ATP binding and hydrolysis at two nucleotide binding domains on each ClpA monomer. We previously reported a molecular mechanism for ClpA catalyzed polypeptide translocation in the absence of ClpP, including elementary rate constants, overall rate, and the kinetic step size. However, the potential allosteric effect of ClpP on the mechanism of ClpA catalyzed translocation remains unclear. Using single-turnover fluorescence stopped-flow methods, here we report that ClpA, when associated with ClpP, translocates polypeptide with an overall rate of ~35 aa s(-1) and, on average, traverses ~5 aa between two rate-limiting steps with reduced cooperativity between ATP binding sites in the hexameric ring. This is in direct contrast to our previously reported observation that, in the absence of ClpP, ClpA translocates polypeptide substrates with a maximum translocation rate of ~20 aa s(-1) with cooperativity between ATPase sites. Our results demonstrate that ClpP allosterically impacts the polypeptide translocation activity of ClpA by reducing the cooperativity between ATP binding sites.
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