ArticlePLoS computational biology2015
Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones.
Article in PLoS computational biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 70 citations in OpenAlex.
- Emergent 3D genome reorganization and graded gene control from the stepwise assembly of transcriptional condensates.Cell reports · 2026Article
- Impact of phylogeny on the inference of functional sectors from protein sequence data.PLoS computational biology · 2024Article
- Functional effects of mutations in proteins can be predicted and interpreted by guided selection of sequence covariation information.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Impact of phylogeny on structural contact inference from protein sequence data.Journal of the Royal Society, Interface · 2023Article
- Correlations from structure and phylogeny combine constructively in the inference of protein partners from sequences.PLoS computational biology · 2022Article
- Extracting phylogenetic dimensions of coevolution reveals hidden functional signals.Scientific reports · 2022Article
- Improving sequence-based modeling of protein families using secondary-structure quality assessment.Bioinformatics (Oxford, England) · 2021Article
- Conformational equilibria in allosteric control of Hsp70 chaperones.Molecular cell · 2021Article
- The Hsp70-Chaperone Machines in Bacteria.Frontiers in molecular biosciences · 2021Review
- Protein Structural Information and Evolutionary Landscape by In Vitro Evolution.Molecular biology and evolution · 2020Article
- Epistatic contributions promote the unification of incompatible models of neutral molecular evolution.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Coevolutionary Analysis of Protein Subfamilies by Sequence Reweighting.Entropy (Basel, Switzerland) · 2020Article
- Coevolutionary Couplings Unravel PAM-Proximal Constraints of CRISPR-SpCas9.Biophysical journal · 2019Article
- Phylogenetic correlations can suffice to infer protein partners from sequences.PLoS computational biology · 2019Article
- Revealing evolutionary constraints on proteins through sequence analysis.PLoS computational biology · 2019Article
- Article
- Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones.The Journal of biological chemistry · 2019Review
- Human Stress-inducible Hsp70 Has a High Propensity to Form ATP-dependent Antiparallel Dimers That Are Differentially Regulated by Cochaperone Binding.Molecular & cellular proteomics : MCP · 2019Article
- Oligomerization of Hsp70: Current Perspectives on Regulation and Function.Frontiers in molecular biosciences · 2019Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hsp70s are a class of ubiquitous and highly conserved molecular chaperones playing a central role in the regulation of proteostasis in the cell. Hsp70s assist a myriad of cellular processes by binding unfolded or misfolded substrates during a complex biochemical cycle involving large-scale structural rearrangements. Here we show that an analysis of coevolution at the residue level fully captures the characteristic large-scale conformational transitions of this protein family, and predicts an evolutionary conserved-and thus functional-homo-dimeric arrangement. Furthermore, we highlight that the features encoding the Hsp70 dimer are more conserved in bacterial than in eukaryotic sequences, suggesting that the known Hsp70/Hsp110 hetero-dimer is a eukaryotic specialization built on a pre-existing template.
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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.