ArticleThe Journal of biological chemistry2017
Structural model of dodecameric heat-shock protein Hsp21: Flexible N-terminal arms interact with client proteins while C-terminal tails maintain the dodecamer and chaperone activity.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Stress resilience in plants: the complex interplay between heat stress memory and resetting.The New phytologist · 2025Review
- MoBiFC: development of a modular bimolecular fluorescence complementation toolkit for the analysis of chloroplast protein-protein interactions.Plant methods · 2022Article
- SARS-CoV-2 spike evolutionary behaviors; simulation of N501Y mutation outcomes in terms of immunogenicity and structural characteristic.Journal of cellular biochemistry · 2022Article
- Multiple nanocages of a cyanophage small heat shock protein with icosahedral and octahedral symmetries.Scientific reports · 2021Article
- JMJ Histone Demethylases Balance H3K27me3 and H3K4me3 Levels at theBiomolecules · 2021Article
- Structural basis of substrate recognition and thermal protection by a small heat shock protein.Nature communications · 2021Article
- Cryo-EM structures of engineered active bcNature communications · 2021Article
- The Chloroplastic Small Heat Shock Protein GeneInternational journal of genomics · 2021Article
- The Mitochondrial Small Heat Shock Protein HSP22 from Pea is a Thermosoluble Chaperone Prone to Co-Precipitate with Unfolding Client Proteins.International journal of molecular sciences · 2019Article
- Evolving SAXS versatility: solution X-ray scattering for macromolecular architecture, functional landscapes, and integrative structural biology.Current opinion in structural biology · 2019Review
- Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface.Scientific reports · 2018Article
- Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state.Nature communications · 2017Article
- The chloroplast-localized small heat shock protein Hsp21 associates with the thylakoid membranes in heat-stressed plants.Protein science : a publication of the Protein Society · 2017Article
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small heat-shock proteins (sHsps) prevent aggregation of thermosensitive client proteins in a first line of defense against cellular stress. The mechanisms by which they perform this function have been hard to define due to limited structural information; currently, there is only one high-resolution structure of a plant sHsp published, that of the cytosolic Hsp16.9. We took interest in Hsp21, a chloroplast-localized sHsp crucial for plant stress resistance, which has even longer N-terminal arms than Hsp16.9, with a functionally important and conserved methionine-rich motif. To provide a framework for investigating structure-function relationships of Hsp21 and understanding these sequence variations, we developed a structural model of Hsp21 based on homology modeling, cryo-EM, cross-linking mass spectrometry, NMR, and small-angle X-ray scattering. Our data suggest a dodecameric arrangement of two trimer-of-dimer discs stabilized by the C-terminal tails, possibly through tail-to-tail interactions between the discs, mediated through extended I
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