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J. Bacteriol., Aug 1995, 4593-4600, Vol 177, No. 16
Copyright © 1995, American Society for Microbiology

Mutation of the Ser2 codon of the light-harvesting B870 alpha polypeptide of Rhodobacter capsulatus partially suppresses the pufX phenotype

TG Lilburn, RC Prince and JT Beatty
Department of Microbiology and Immunology, University of British Columbia, Vancouver, Canada.

The exact function of the pufX gene product of Rhodobacter capsulatus is uncertain, but deletion of the pufX gene renders cells incapable of phototrophic growth on a minimal medium, and photosynthetic electron transfer is impaired in vitro. However, suppressor mutants that are able to grow phototropically are readily isolated. Two such suppressor mutants were characterized as to their phototrophic growth properties, their fluorescence at different incident light intensities, the integrity of their chromatophores, and their abilities to generate a transmembrane potential. We found that the photosynthetic apparatus in the suppressor mutants was less stable than that of the pseudo-wild- type and primary mutant strains and that the suppressor mutants used light energy less efficiently than the pseudo-wild-type strain. Therefore, the suppressor strains are more precisely designated partial suppressor mutants. The locations and sequences of the suppressor mutations were determined, and both were found to change the second codon of the pufA gene. It is hypothesized that the serine residue specified by this codon is important in interactions between the B870 alpha protein and other membrane-bound polypeptides and that suppressor mutations at this position partially compensate for loss of the PufX protein. A model is proposed for the function of the PufX protein.

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