ArticleProtein science : a publication of the Protein Society2007
Chemical cross-linking of the chloroplast localized small heat-shock protein, Hsp21, and the model substrate citrate synthase.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed.
- Small heat shock protein HSPB8 interacts with a pre-fibrillar TDP43 low complexity domain species to delay fibril formation.Biophysical chemistry · 2026Article
- The role of heat shock proteins in preventing amyloid toxicity.Frontiers in molecular biosciences · 2022Review
- Structural basis of substrate recognition and thermal protection by a small heat shock protein.Nature communications · 2021Article
- Proteinaceous Transformers: Structural and Functional Variability of Human sHsps.International journal of molecular sciences · 2020Review
- 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
- Chaperone-like activity of the N-terminal region of a human small heat shock protein and chaperone-functionalized nanoparticles.Proteins · 2019Article
- Small heat shock proteins: Simplicity meets complexity.The Journal of biological chemistry · 2019Review
- The growing world of small heat shock proteins: from structure to functions.Cell stress & chaperones · 2017Review
- 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.The Journal of biological chemistry · 2017Article
- Structural and functional consequences of chaperone site deletion in αA-crystallin.Biochimica et biophysica acta · 2016Article
- Characterization of rice small heat shock proteins targeted to different cellular organelles.Cell stress & chaperones · 2015Article
- A first line of stress defense: small heat shock proteins and their function in protein homeostasis.Journal of molecular biology · 2015Review
- Algae sense exact temperatures: small heat shock proteins are expressed at the survival threshold temperature in Cyanidioschyzon merolae and Chlamydomonas reinhardtii.Genome biology and evolution · 2014Article
- Regulated structural transitions unleash the chaperone activity of αB-crystallin.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Probing the transient interaction between the small heat-shock protein Hsp21 and a model substrate protein using crosslinking mass spectrometry.Cell stress & chaperones · 2013Article
- Overexpression of small heat shock protein LimHSP16.45 in Arabidopsis enhances tolerance to abiotic stresses.PloS one · 2013Article
- Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions.Trends in biochemical sciences · 2012Article
- Article
- Thiol-exchange in DTSSP crosslinked peptides is proportional to cysteine content and precisely controlled in crosslink detection by two-step LC-MALDI MSMS.Protein science : a publication of the Protein Society · 2011Article
- Subunit arrangement in the dodecameric chloroplast small heat shock protein Hsp21.Protein science : a publication of the Protein Society · 2011Article
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5 authors.
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Abstract
The molecular mechanism whereby the small heat-shock protein (sHsp) chaperones interact with and prevent aggregation of other proteins is not fully understood. We have characterized the sHsp-substrate protein interaction at normal and increased temperatures utilizing a model substrate protein, citrate synthase (CS), widely used in chaperone assays, and a dodecameric plant sHsp, Hsp21, by chemical cross-linking with 3,3'-Dithiobis[sulfosuccinimidylpropionate] (DTSSP) and mass spectrometric peptide mapping. In the absence of CS, the cross-linker captured Hsp21 in dodecameric form, even at increased temperature (47 degrees C). In the presence of equimolar amounts of CS, no Hsp21 dodecamer was captured, indicating a substrate-induced Hsp21 dodecamer dissociation by equimolar amounts of CS. Cross-linked Hsp21-Hsp21 dipeptides indicated an exposure of the Hsp21 C-terminal tails and substrate-binding sites normally covered by the C terminus. Cross-linked Hsp21-CS dipeptides mapped to several sites on the surface of the CS dimer, indicating that there are numerous weak and short-lived interactions between Hsp21 and CS, even at normal temperatures. The N-terminal arms especially interacted with a motif in the CS dimer, which is absent in thermostable forms of CS. The cross-linking data suggest that the presence of substrate rather than temperature influences the conformation of Hsp21.
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