Characterization of the pet operon of Rhodospirillum rubrum
- 1 May 1992
- journal article
- research article
- Published by Springer Nature in Photosynthesis Research
- Vol. 32 (2) , 79-94
- https://doi.org/10.1007/bf00035943
Abstract
The three genes of the pet operon, coding, respectively, for the Rieske iron-sulfur protein, cytochrome b and cytochrome c1 components of the cytochrome bc1 complex in the photosynthetic bacterium Rhodospirillum rubrum have been sequenced. The amino acid sequences deduced for these three peptides from the nucleotide sequences of the genes have been confirmed, in part, by direct sequencing of portions of the three peptides separated from a sample of the purified, detergent-solubilized complex. These sequences show considerable homology with those previously obtained for the pet operons of other photosynthetic bacteria. Northern blots of R. rubrum mRNA have established that the operon is transcribed as a single polycistronic message, the start site of which has been determined by both primer extension and nuclease protection. Photosynthetic growth of R. rubrum was shown to be inhibited by antimycin A, a specific inhibitor of cytochrome bc1 complexes, and antimycin A-resistant mutants of R. rubrum have been isolated. Preliminary results suggest that it may be possible to express the R. rubrum pet operon in a strain of the photosynthetic bacterium Rhodobacter capsulatus from which the native pet operon has been deleted.Keywords
This publication has 69 references indexed in Scilit:
- Studies on transformation of Escherichia coli with plasmidsPublished by Elsevier ,2006
- Mutational analysis of the mouse mitochondrial cytochrome b geneJournal of Molecular Biology, 1988
- fbc Operon, encoding the Rieske FeS protein cytochrome b, and cytochrome c1 apoproteins previously described from Rhodopseudomonas sphaeroides, is from Rhodopseudomonas capsulataJournal of Molecular Biology, 1987
- Primary structure of the bc1 complex of Rhodopseudomonas capsulataJournal of Molecular Biology, 1987
- Isolation of the structural genes for the Rieske FeS protein, cytochrome b and cytochrome c1 all components of the ubiquinol: Cytochrome c2 oxidoreductase complex of Rhodopseudomonas capsulataJournal of Molecular Biology, 1987
- Evidence for N coordination to Fe in the [2Fe‐2S] center in yeast mitochondrial complex III Comparison with similar findings for analogous bacterial [2Fe‐2S] proteinsFEBS Letters, 1987
- Reduction of cytochrome b‐561 through the antimycin‐sensitive site of the ubiquinol‐cytochrome c2 oxidoreductase complex of Rhodopseudomonas sphaeroidesFEBS Letters, 1984
- Comparative aspects of quinol-cytochrome c/plastocyanin oxidoreductasesBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1983
- A Cytochrome f/b6 Complex of Five Polypeptides with Plastoquinol‐Plastocyanin‐Oxidoreductase Activity from Spinach ChloroplastsEuropean Journal of Biochemistry, 1981
- A Requirement for Sodium in the Growth of Rhodopseudomonas spheroidesJournal of General Microbiology, 1960