ArticleProceedings of the National Academy of Sciences of the United States of America2001
ClpA mediates directional translocation of substrate proteins into the ClpP protease.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 149 citations in OpenAlex.
- Regulation of the Anti-termination RNA Transcription Complex by Lon-Mediated Lambda N Degradation.Advances in experimental medicine and biology · 2026Review
- Single turnover transient state kinetics reveals processive protein unfolding catalyzed byeLife · 2024Article
- AAA+ proteins: one motor, multiple ways to work.Biochemical Society transactions · 2022Review
- General Structural and Functional Features of Molecular Chaperones.Advances in experimental medicine and biology · 2021Article
- Kinetic Analysis of AAA+ Translocases by Combined Fluorescence and Anisotropy Methods.Biophysical journal · 2020Article
- The Intrinsically Disordered N-terminal Extension of the ClpS Adaptor Reprograms Its Partner AAA+ ClpAP Protease.Journal of molecular biology · 2020Article
- Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis.Nature structural & molecular biology · 2020Article
- Role of Heat Shock Proteases in Quorum-Sensing-Mediated Regulation of Biofilm Formation bymBio · 2018Article
- Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions.Frontiers in molecular biosciences · 2017Review
- Article
- Escherichia coli ClpB is a non-processive polypeptide translocase.The Biochemical journal · 2015Article
- Cleavage Specificity of Mycobacterium tuberculosis ClpP1P2 Protease and Identification of Novel Peptide Substrates and Boronate Inhibitors with Anti-bacterial Activity.The Journal of biological chemistry · 2015Article
- Lipopeptide biosynthesis in Pseudomonas fluorescens is regulated by the protease complex ClpAP.BMC microbiology · 2015Article
- Quantitative genome-wide genetic interaction screens reveal global epistatic relationships of protein complexes in Escherichia coli.PLoS genetics · 2014Article
- ATPγS competes with ATP for binding at Domain 1 but not Domain 2 during ClpA catalyzed polypeptide translocation.Biophysical chemistry · 2014Article
- E. coli ClpA catalyzed polypeptide translocation is allosterically controlled by the protease ClpP.Journal of molecular biology · 2013Article
- Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triad.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- ClpS1 is a conserved substrate selector for the chloroplast Clp protease system in Arabidopsis.The Plant cell · 2013Article
- Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Aggregate reactivation mediated by the Hsp100 chaperones.Archives of biochemistry and biophysics · 2012Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The intracellular degradation of many proteins is mediated in an ATP-dependent manner by large assemblies comprising a chaperone ring complex associated coaxially with a proteolytic cylinder, e.g., ClpAP, ClpXP, and HslUV in prokaryotes, and the 26S proteasome in eukaryotes. Recent studies of the chaperone ClpA indicate that it mediates ATP-dependent unfolding of substrate proteins and directs their ATP-dependent translocation into the ClpP protease. Because the axial passageway into the proteolytic chamber is narrow, it seems likely that unfolded substrate proteins are threaded from the chaperone into the protease, suggesting that translocation could be directional. We have investigated directionality in the ClpA/ClpP-mediated reaction by using two substrate proteins bearing the COOH-terminal ssrA recognition element, each labeled near the NH(2) or COOH terminus with fluorescent probes. Time-dependent changes in both fluorescence anisotropy and fluorescence resonance energy transfer between donor fluorophores in the ClpP cavity and the substrate probes as acceptors were measured to monitor translocation of the substrates from ClpA into ClpP. We observed for both substrates that energy transfer occurs 2--4 s sooner with the COOH-terminally labeled molecules than with the NH(2)-terminally labeled ones, indicating that translocation is indeed directional, with the COOH terminus of the substrate protein entering ClpP first.
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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.