Localization of a multifunctional chaperonin (GroEL protein) in nitrogen-fixing Anabaena PCC 7120
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- Jāger, K.M. & Bergman, B. Planta (1991) 183: 120. doi:10.1007/BF00197575
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The occurrence and distribution of a multifunctional chaperonin-60 (cpn60), the GroEL protein, was demonstrated in the cyanobacterium Anabaena PCC 7120 by using a rabbit anti-GroEL (Escherichia coli) antibody. Western-blot analysis showed a distinct cross-reaction with a protein of approx. 65 kilodaltons, analogous to the Mr of the E. coli homologue. Immunocyto-chemical studies of vegetative cells showed that a chaperonin was localized in both vegetative cells and heterocysts. In vegetative cells cpn60 was primarily detected both in the carboxysomes, and in the cytoplasm, though mainly in the thylakoid region of the latter. In heterocysts, specialized cells for nitrogen fixation, the cpn60 label was prominent and was evenly distributed throughout the cell. These results support recent findings that chaperonins are multifunctional proteins, and extend those findings by demonstrating the occurrence of cpn60 in a prokaryotic cyanobacterium and by raising the possibility of the involvement of this chaperonin in the assembly of heterocystous proteins.
Key wordsAnabaena Chaperonin localization GroEL protein Nitrogenase Ribulose-1,5-bisphosphate carboxylase/oxygenase
relative molecular mass