ArticlePlant physiology1998
The chloroplast small heat-shock protein oligomer is not phosphorylated and does not dissociate during heat stress in vivo.
Article in Plant physiology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- 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
- Characterization of rice small heat shock proteins targeted to different cellular organelles.Cell stress & chaperones · 2015Article
- A low molecular weight proteome comparison of fertile and male sterile 8 anthers of Zea mays.Plant biotechnology journal · 2012Article
- Phylogenetic and biochemical studies reveal a potential evolutionary origin of small heat shock proteins of animals from bacterial class A.Journal of molecular evolution · 2006Article
- Plant responses to drought, salinity and extreme temperatures: towards genetic engineering for stress tolerance.Planta · 2003Review
- Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.Microbiology and molecular biology reviews : MMBR · 2002Review
- Chloroplast small heat shock proteins: evidence for atypical evolution of an organelle-localized protein.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Methionine sulfoxidation of the chloroplast small heat shock protein and conformational changes in the oligomer.Protein science : a publication of the Protein Society · 1999Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Plants synthesize several classes of small (15- to 30-kD monomer) heat-shock proteins (sHSPs) in response to heat stress, including a nuclear-encoded, chloroplast-localized sHSP (HSP21). Cytosolic sHSPs exist as large oligomers (approximately 200-800 kD) composed solely or primarily of sHSPs. Phosphorylation of mammalian sHSPs causes oligomer dissociation, which appears to be important for regulation of sHSP function. We examined the native structure and phosphorylation of chloroplast HSP21 to understand this protein's basic properties and to compare it with cytosolic sHSPs. The apparent size of native HSP21 complexes was > 200 kD and they did not dissociate during heat stress. We found no evidence that HSP21 or the plant cytosolic sHSPs are phosphorylated in vivo. A partial HSP21 complex purified from heat-stressed pea (Pisum sativum L.) leaves contained no proteins other than HSP21. Mature recombinant pea and Arabidopsis thaliana HSP21 were expressed in Escherichia coli, and purified recombinant Arabidopsis HSP21 assembled into homo-oligomeric complexes with the same apparent molecular mass as HSP21 complexes observed in heat-stressed leaf tissue. We propose that the native, functional form of chloroplast HSP21 is a large, oligomeric complex containing nine or more HSP21 subunits, and that plant sHSPs are not regulated by phosphorylation-induced dissociation.
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