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J. Biol. Chem., Vol. 263, Issue 16, 7632-7638, Jun, 1988

The structural genes coding for the L and M subunits of Rhodospirillum rubrum photoreaction center

G Belanger, J Berard, P Corriveau and G Gingras
Departement de Biochimie, Universite de Montreal, Quebec, Canada.

In Rhodospirillum rubrum, pufL, and pufM, the structural genes coding for the photoreaction center L and M polypeptides, are comprised respectively of 831 and 921 nucleotides. They are separated by a stretch of 12 nucleotides between the TAA stop codon of pufL and the first base of the ATG initiation codon of pufM. The predicted amino acid sequence of the L and M polypeptides, respectively, contain 275 and 305 residues with corresponding molecular weights of 30,473 and 33,978. Their sequences are highly homologous to those of Rhodobacter sphaeroides, Rhodobacter capsulatus, and Rhodopseudomonas viridis. As can be deduced from the crystallographic structure of other photoreaction centers, the regions of greatest similarity are the binding sites of the cofactors involved in the photochemical reaction rather than the protein secondary structure. L and M contain, at conserved positions of their sequences, three main clusters of positively charged residues on the cytoplasmic side of the membrane. This arrangement may be involved in protein orientation during membrane assembly. Evolutionary distance of pufL and pufM, as assessed by substitution frequency analysis, confirms the closeness of the two Rhodobacter species, the other two species being equidistant from one another. Interspecies evolutionary distance is greater for pufL than for pufM.
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