Abstract
Six isolates of the purple non-sulfur bacteria, which upon primary isolation were naturally resistant to the herbicide atrazine, were characterized with respect to their taxonomic identity and the mechanism of their resistance. On the basis of electron microscopy, photopigment analysis, and other criteria, they were identified as strains of Rhodopseudomonas acidophila, Rhodopseudomonas palustris, or Rhodocyclus gelatinosus. These isolates exhibited degrees of atrazine resistance which ranged from 1.5 to about 4 times greater than that of cognate reference strains (American Type Culture Collection) tested. Furthermore, all of the reference strains tested were more intrinsically resistant to atrazine than was Rhodobacter sphaeroides. No unique plasmids which might encode for herbicide degradation or inactivation were found in these isolates. Resistance to the herbicide in these isolates was not the result of diminished binding of the herbicide to the L subunit of the bacterial reaction center. Differences in herbicide resistance among the various species of this group may be the result of compositional and chemical differences in the individual reaction centers. However, the increase in atrazine resistance for the isolates characterized in this study probably occurs by undefined mechanisms and not necessarily by changes in the binding of the herbicide to the L subunit of the photosynthetic reaction center.
Full text
PDF






Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Birnboim H. C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979 Nov 24;7(6):1513–1523. doi: 10.1093/nar/7.6.1513. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brown A. E., Eiserling F. A., Lascelles J. Bacteriochlorophyll Synthesis and the Ultrastructure of Wild Type and Mutant Strains of Rhodopseudomonas spheroides. Plant Physiol. 1972 Dec;50(6):743–746. doi: 10.1104/pp.50.6.743. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brown A. E., Gilbert C. W., Guy R., Arntzen C. J. Triazine herbicide resistance in the photosynthetic bacterium Rhodopseudomonas sphaeroides. Proc Natl Acad Sci U S A. 1984 Oct;81(20):6310–6314. doi: 10.1073/pnas.81.20.6310. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Campbell A. Evolutionary significance of accessory DNA elements in bacteria. Annu Rev Microbiol. 1981;35:55–83. doi: 10.1146/annurev.mi.35.100181.000415. [DOI] [PubMed] [Google Scholar]
- Erickson J. M., Rahire M., Rochaix J. D., Mets L. Herbicide resistance and cross-resistance: changes at three distinct sites in the herbicide-binding protein. Science. 1985 Apr 12;228(4696):204–207. doi: 10.1126/science.228.4696.204. [DOI] [PubMed] [Google Scholar]
- Galloway R. E., Mets L. J. Atrazine, bromacil, and diuron resistance in chlamydomonas: a single non-mendelian genetic locus controls the structure of the thylakoid binding site. Plant Physiol. 1984 Mar;74(3):469–474. doi: 10.1104/pp.74.3.469. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gibson K. D., Niederman R. A. Characterization of two circular satellite species of deoxyribonucleic acid in Rhodopseudomonas spheroides. Arch Biochem Biophys. 1970 Dec;141(2):694–704. doi: 10.1016/0003-9861(70)90190-6. [DOI] [PubMed] [Google Scholar]
- Golden S. S., Haselkorn R. Mutation to herbicide resistance maps within the psbA gene of Anacystis nidulans R2. Science. 1985 Sep 13;229(4718):1104–1107. doi: 10.1126/science.3929379. [DOI] [PubMed] [Google Scholar]
- Haworth P., Steinback K. E. Interaction of Herbicides and Quinone with the Q(B)-Protein of the Diuron-Resistant Chlamydomonas reinhardtii Mutant Dr2. Plant Physiol. 1987 Apr;83(4):1027–1031. doi: 10.1104/pp.83.4.1027. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hirschberg J., McIntosh L. Molecular Basis of Herbicide Resistance in Amaranthus hybridus. Science. 1983 Dec 23;222(4630):1346–1349. doi: 10.1126/science.222.4630.1346. [DOI] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
- Michel H., Weyer K. A., Gruenberg H., Dunger I., Oesterhelt D., Lottspeich F. The 'light' and 'medium' subunits of the photosynthetic reaction centre from Rhodopseudomonas viridis: isolation of the genes, nucleotide and amino acid sequence. EMBO J. 1986 Jun;5(6):1149–1158. doi: 10.1002/j.1460-2075.1986.tb04340.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pfister K., Steinback K. E., Gardner G., Arntzen C. J. Photoaffinity labeling of an herbicide receptor protein in chloroplast membranes. Proc Natl Acad Sci U S A. 1981 Feb;78(2):981–985. doi: 10.1073/pnas.78.2.981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Stein R. R., Castellvi A. L., Bogacz J. P., Wraight C. A. Herbicide-quinone competition in the acceptor complex of photosynthetic reaction centers from Rhodopseudomonas sphaeroides: a bacterial model for PS-II-herbicide activity in plants. J Cell Biochem. 1984;24(3):243–259. doi: 10.1002/jcb.240240306. [DOI] [PubMed] [Google Scholar]
- Williams J. C., Steiner L. A., Feher G., Simon M. I. Primary structure of the L subunit of the reaction center from Rhodopseudomonas sphaeroides. Proc Natl Acad Sci U S A. 1984 Dec;81(23):7303–7307. doi: 10.1073/pnas.81.23.7303. [DOI] [PMC free article] [PubMed] [Google Scholar]



