ArticlePlant physiology1997
Purification and in vitro chaperone activity of a class I small heat-shock protein abundant in recalcitrant chestnut seeds.
Article in Plant physiology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 54 citations in OpenAlex.
- Article
- The CsHSP17.2 molecular chaperone is essential for thermotolerance in Camellia sinensis.Scientific reports · 2017Article
- Differentially expressed seed aging responsive heat shock protein OsHSP18.2 implicates in seed vigor, longevity and improves germination and seedling establishment under abiotic stress.Frontiers in plant science · 2015Article
- Plantation forestry under global warming: hybrid poplars with improved thermotolerance provide new insights on the in vivo function of small heat shock protein chaperones.Plant physiology · 2014Article
- The molecular basis for stress-induced acquisition of somatic embryogenesis.Molecular biology reports · 2010Review
- Non-redundant functions of sHSP-CIs in acquired thermotolerance and their role in early seed development in Arabidopsis.Plant molecular biology · 2008Article
- Molecular chaperone activity of tomato (Lycopersicon esculentum) endoplasmic reticulum-located small heat shock protein.Journal of plant research · 2008Article
- From Avicennia to Zizania: seed recalcitrance in perspective.Annals of botany · 2008Article
- Protein cryoprotective activity of a cytosolic small heat shock protein that accumulates constitutively in chestnut stems and is up-regulated by low and high temperatures.Plant physiology · 2004Article
- Plant responses to drought, salinity and extreme temperatures: towards genetic engineering for stress tolerance.Planta · 2003Review
- Article
- Heterologous expression of a plant small heat-shock protein enhances Escherichia coli viability under heat and cold stress.Plant physiology · 1999Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A 20-kD protein has been purified from cotyledons of recalcitrant (desiccation-sensitive) chestnut (Castanea sativa) seeds, where it accumulates at levels comparable to those of major seed storage proteins. This protein, termed Cs smHSP 1, forms homododecameric complexes under nondenaturing conditions and appears to be homologous to cytosolic class I small heat-shock proteins (smHSPs) from plant sources. In vitro evidence has been obtained that the isolated protein can function as a molecular chaperone; it increases, at stoichiometric levels, the renaturation yields of chemically denatured citrate synthase and also prevents the irreversible thermal inactivation of this enzyme. Although a role in desiccation tolerance has been hypothesized for seed smHSPs, this does not seem to be the case for Cs smHSP 1. We have investigated the presence of immunologically related proteins in orthodox and recalcitrant seeds of 13 woody species. Our results indicate that the presence of Cs smHSP 1-like proteins, even at high levels, is not enough to confer desiccation tolerance, and that the amount of these proteins does not furnish a reliable criterion to identify desiccation-sensitive seeds. Additional proteins or mechanisms appear necessary to keep the viability of orthodox seeds upon shedding.
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