ArticlePlant physiology1992
The identification of a heat-shock protein complex in chloroplasts of barley leaves.
Article in Plant physiology, 1992. 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, 45 citations in OpenAlex.
- Structure and function of a novel type of ATP-dependent Clp protease.The Journal of biological chemistry · 2009Article
- Structural and functional insights into the chloroplast ATP-dependent Clp protease in Arabidopsis.The Plant cell · 2006Article
- The chloroplast small heat-shock protein oligomer is not phosphorylated and does not dissociate during heat stress in vivo.Plant physiology · 1998Article
- The cyanobacterium Synechococcus resists UV-B by exchanging photosystem II reaction-center D1 proteins.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Induction of the heat shock protein ClpB affects cold acclimation in the cyanobacterium Synechococcus sp. strain PCC 7942.Journal of bacteriology · 1997Article
- Folate biosynthesis in higher plants: purification and molecular cloning of a bifunctional 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8-dihydropteroate synthase localized in mitochondria.The EMBO journal · 1997Article
- The heat shock protein ClpB mediates the development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942.Journal of bacteriology · 1996Article
- The cyanobacterium Synechococcus sp. PCC 7942 possesses a close homologue to the chloroplast ClpC protein of higher plants.Plant molecular biology · 1996Article
- Electron transport regulates exchange of two forms of photosystem II D1 protein in the cyanobacterium Synechococcus.The EMBO journal · 1995Article
- Purification and characterisation of an intracellular carbonic anhydrase from the unicellular green alga Coccomyxa.Planta · 1995Article
- A Low Molecular Mass Heat-Shock Protein Is Localized to Higher Plant Mitochondria.Plant physiology · 1994Article
- Two functionally distinct forms of the photosystem II reaction-center protein D1 in the cyanobacterium Synechococcus sp. PCC 7942.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Rapid interchange between two distinct forms of cyanobacterial photosystem II reaction-center protein D1 in response to photoinhibition.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In vivo radiolabeling of chloroplast proteins in barley (Hordeum vulgare L. cv Corvette) leaves and their separation by one-dimensional electrophoresis revealed at least seven heat-shock proteins between 24 and 94 kD, of which most have not been previously identified in this C(3) species. Fractionation into stromal and thylakoid membrane components showed that all chloroplast heat-shock proteins were synthesized on cytoplasmic ribosomes, translocated into the chloroplast, and located in the stroma. Examination of stromal preparations by native (nondissociating) polyacrylamide gel electrophoresis revealed the presence of a high-molecular mass heat-shock protein complex in barley. This complex was estimated to be 250 to 265 kD in size. Dissociation by denaturing polyacrylamide gel electrophoresis revealed a single protein component, a 32-kD heat-shock protein. The synthesis of this protein and the formation of the heat-shock protein complex were dependent on functional cytoplasmic ribosomes. Immunological studies showed that the heat-shock protein complex did not contain any proteins homologous to the alpha-subunit of ribulose bisphosphate carboxylase oxygenase subunit-binding protein. Other features about the complex included the absence of nucleic acid (RNA or DNA) and its nondissociation in the presence of Mg(2+)/ATP. These results suggest that the heat-shock protein complex in barley chloroplasts is a homogeneous octamer of 32-kD subunits.
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