Structure and transcription of the genes encoding the B1015 light-harvesting complex beta and alpha subunits and the photosynthetic reaction center L, M, and cytochrome c subunits from Rhodopseudomonas viridis.

The genes encoding the beta and alpha subunits of the B1015 light-harvesting complex (LHC) and the L, M, and cytochrome c subunits of the photosynthetic reaction center from Rhodopseudomonas viridis are organized in an operon, in analogy to other nonsulfur purple bacteria, named the puf operon. In photoheterotrophically grown cells, two abundant puf operon mRNA species of 3,581 and 621 bases were present. The large transcript encoded the LHC beta, LHC alpha, and reaction center L, M, and cytochrome c polypeptides, whereas the small transcript only coded for the LHC beta and alpha polypeptides. Both transcripts share a common 5' end which is located 115 bases upstream from the initiation codon of the LHC beta gene. Two additional low-level transcripts of 3,718 and 758 bases with 5' ends 254 +/- 3 bases upstream from the LHC beta gene were detected. Analysis of the DNA sequence preceding the different 5' ends revealed DNA elements of striking homology. The 3' ends of the small transcripts were mapped within the alpha-L intercistronic DNA region downstream from a sequence capable of forming a very stable stem-loop when transcribed into RNA. The 3' termini of the large transcripts are located immediately downstream from the region coding the cytochrome c subunit in two areas resembling rho-independent transcription terminators. No open reading frames corresponding to pufQ and pufX from Rhodobacter capsulatus and Rhodobacter sphaeroides were present in the flanking DNA regions of the puf operon. In contrast, an open reading frame ending 191 base pairs upstream from the LHC beta gene showed 50% homology at the amino acid level to the available sequence of the bchA gene from R. capsulatus. The genes coding for the B1015 LHC subunits had C-terminal extensions of 13 (beta) and 10 (alpha) amino acids which were not present in the proteins isolated from intracytoplasmic membranes.