ArticleBiophysical journal2020
The Anti-Aggregation Holdase Hsp33 Promotes the Formation of Folded Protein Structures.
Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Systematic enhancement of protein crystallization efficiency by bulk lysine-to-arginine (KR) substitution.Protein science : a publication of the Protein Society · 2024Article
- G-quadruplexes rescuing protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Optimized Microscale Protein Aggregation Suppression Assay: A Method for Evaluating the Holdase Activity of Chaperones.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Single-molecule mechanical studies of chaperones and their clients.Biophysics reviews · 2022Review
- Trigger factor both holds and folds its client proteins.Nature communications · 2022Article
- Article
- Proteomic and Transcriptomic Analysis ofmSystems · 2021Article
- Bacterial Defense Systems against the Neutrophilic Oxidant Hypochlorous Acid.Infection and immunity · 2020Review
- TrypOx, a Novel Eukaryotic Homolog of the Redox-Regulated Chaperone Hsp33 inFrontiers in microbiology · 2020Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Holdase chaperones are known to be central to suppressing aggregation, but how they affect substrate conformations remains poorly understood. Here, we use optical tweezers to study how the holdase Hsp33 alters folding transitions within single maltose binding proteins and aggregation transitions between maltose binding protein substrates. Surprisingly, we find that Hsp33 not only suppresses aggregation but also guides the folding process. Two modes of action underlie these effects. First, Hsp33 binds unfolded chains, which suppresses aggregation between substrates and folding transitions within substrates. Second, Hsp33 binding promotes substrate states in which most of the chain is folded and modifies their structure, possibly by intercalating its intrinsically disordered regions. A statistical ensemble model shows how Hsp33 function results from the competition between these two contrasting effects. Our findings reveal an unexpectedly comprehensive functional repertoire for Hsp33 that may be more prevalent among holdases and dispels the notion of a strict chaperone hierarchy.
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Registered trials
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