Cytochrome b-559 genes from Oenothera hookeri and Nicotiana tabacum show a remarkably high degree of conservation as compared to spinach. The enigma of cytochrome b-559: highly conserved genes and proteins but no known function.

Recent data suggest that cytochrome b-559, an intrinsic membrane protein of the oxygen-evolving photosystem II in chloroplasts, is a heme cross-linked heteromeric polypeptide unit (Herrmann et al. 1984, FEBS Lett 176:239-244). The genes for this cytochrome, designated psbE and psbF, have been located on the chloroplast chromosome of Oenothera hookeri and Nicotiana tabacum by hybridization with fragments of the corresponding spinach genes, and characterized. In both cases, the nucleotide sequence discloses 2 uninterrupted reading frames of 83 and 39 codons separated by a few nucleotides, as in spinach. The amber translation stop codon of psbE overlaps the putative ribosome-binding site for psbF in all cases. The predicted molecular weights of the proteins are 9.2 and 4.3 kd, respectively. In each of the three plant species, and the direction of transcription is opposite to that of the gene for cytochrome f which is located distal to the b-559 genes. Comparison of the deduced amino acid sequences with those from the corresponding spinach genes shows 97% homology. The ubiquitous presence and remarkably high degree of structural and functional conservation of this gene cluster supports the hypothesis of a heteromeric assembly and an important functional role for cytochrome b-559.