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• W1980089232 abstract "Higher plant chloroplasts contain two chaperonin 60 family proteins, Cpn60α and Cpn60β, which are known to have divergent amino acid sequences. Although Cpn60α and Cpn60β are present in roughly equal amounts and copurify in their native states, a heterogeneous ensemble of the chaperonin oligomer has not yet been demonstrated. We separately purified Cpn60α and Cpn60β proteins from spinach leaves as the monomeric form. Either antibody raised against one chaperonin 60 protein could coimmunoprecipitate the other chaperonin 60 protein in their oligomeric state but not in its monomeric state, suggesting that the chloroplast Cpn60α and Cpn60β polypeptides actually reside in the same chaperonin oligomer in the stroma. Moreover, the chaperonin oligomers migrated as at least two distinct bands on the native gel electrophoresis, each of which contained both chaperonin 60 proteins. These results suggest that chloroplast chaperonin oligomers might be composed of at least two distinct sets of two chaperonin proteins." @default.
• W1980089232 created "2016-06-24" @default.
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• W1980089232 creator A5050980244 @default.
• W1980089232 creator A5078553283 @default.
• W1980089232 date "1999-12-01" @default.
• W1980089232 modified "2023-09-27" @default.
• W1980089232 title "Chloroplast Chaperonins: Evidence for Heterogeneous Assembly of α and β Cpn60 Polypeptides into a Chaperonin Oligomer" @default.
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• W1980089232 doi "https://doi.org/10.1006/bbrc.1999.1868" @default.
• W1980089232 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10600546" @default.
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