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Protein evolution in cyanobacteria

Nature volume 263, pages 793–796 (1976)Cite this article

Abstract

THERE has been a great deal written in recent years on evolutionary relationships between prokaryotes and eukaryotes1,2, and the possible origin of photosynthesis in eukaryotic cells by endosymbiosis of a cyanobacterium2,3. Molecular methods have been used in an attempt to elucidate the principal events in Precambrian cellular evolution. For example primary structures of plastocyanin4, cytochrome f5, and ferredoxin6,7 have been published. These sequences have been compared to primary structures of functionally analogous macromolecules from eukaryotes. Before conclusions on the evolutionary relationships between prokaryotic cyanobacteria and eukaryotic algae and plants can be made from one representative amino acid sequence, it is necessary to evaluate the amount of amino acid sequence variation in proteins isolated from a wide range of cyanobacteria. In this study the amount of variation in plastocyanins and in cytochromes f was investigated. The results from complete and partial amino acid sequence determinations on these proteins from a number of cyanobacteria, suggest that the rate of evolution of the proteins in oxygenic photosynthetic prokaryotes is much less than the rates of evolution of corresponding proteins in eukaryotic algae and higher plants.

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  1. ALASTAIR AITKEN

    Present address: Service de Physiologie Microbienne, Institut Pasteur, 28, rue du Docteur Roux, 75015, Paris, France

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  1. Department of Molecular Biology, University of Edinburgh, Edinburgh, EH9 3JR, UK

    ALASTAIR AITKEN

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AITKEN, A. Protein evolution in cyanobacteria. Nature 263, 793–796 (1976). https://doi.org/10.1038/263793a0

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