Structural and functional analysis of transcriptional control of the Rhodobacter capsulatus puf operon.
We report data indicating that the Rhodobacter capsulatus puf operon promoter and the site for its oxygen regulation are located more than 700 base pairs upstream from the previously identified puf genes and have identified the nucleotide sequences that constitute these control signals. A model is proposed in which a polycistronic transcript at least 3.4 kilobases in length is initiated near the O2-regulated promoter and is processed posttranscriptionally by endonucleolytic cleavage at multiple sites, yielding discrete mRNA segments that are degraded at different rates. A newly identified gene (pufQ), which includes a hydrophobic domain having some similarity to domains of the products of the pufL and pufM genes, begins 313 nucleotides into the puf transcript and is located entirely within the most rapidly degraded segment of the transcript. A previously identified puf transcript segment encoding structural proteins for photosynthetic membrane complexes persists after degradation of the most 5' region of the transcript and is itself subject to segmentally specific degradation. Our results suggest a model in which differential expression of the multiple genes encoded by the puf operon is at least in part attributable to major differences in the rates of decay of the various segments of puf mRNA.
Adams
C W
CW
Department of Genetics, Stanford University School of Medicine, California 94305.
Forrest
M E
ME
Cohen
S N
SN
Beatty
J T
JT
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D001483:Base Sequence; D005796:Genes; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D009876:Operon; D045322:Photosynthetic Reaction Center Complex Proteins; D011401:Promoter Regions, Genetic; D011487:Protein Conformation; D015183:Restriction Mapping; D012241:Rhodopseudomonas / Q000235:genetics*; D014158:Transcription, Genetic; D001616:beta-Galactosidase
D001426:Bacterial Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D001616:beta-Galactosidase