Abstract
The intrinsic chlorophyll-protein CP 47 is a component of photosystem II which functions in both light-harvesting and oxygen evolution. The large extrinsic loop E of this protein has been shown to interact with the oxygen-evolving site. Previously, Vermaas and coworkers have produced a number of deletions within loop E which yielded mutants which were unable to grow photoautotrophically and which could not evolve oxygen at normal rates. During the course of our site-directed mutagenesis program in Synechocystis 6803, we have altered all of the conserved charged residues which were present within six of these deletions. All ten of these mutants were photoautotrophic and evolved oxygen at normal rates. We speculate that the severe phenotypes of the deletion mutants observed by Vermaas and coworkers in due to large structural perturbations in the extrinsic loop E of CP 47.
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Putnam-Evans, C., Wu, J. & Bricker, T.M. Site-directed mutagenesis of the CP 47 protein of photosystem II: alteration of conserved charged residues which lie within lethal deletions of the large extrinsic loop E. Plant Mol Biol 32, 1191–1195 (1996). https://doi.org/10.1007/BF00041405
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DOI: https://doi.org/10.1007/BF00041405