Characterization of Naturally Occurring Atrazine-resistant Isolates of the Purple Non-sulfur Bacteria

Overview

Journal Appl Environ Microbiol

Specialties Environmental Health
Microbiology

Date 1990 Feb 1

PMID 16348126

Authors

A E Brown

R Luttrell

C T Highfill

A E Rushing

Affiliations

Soon will be listed here.

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.

References

Golden S, Haselkorn R . Mutation to herbicide resistance maps within the psbA gene of Anacystis nidulans R2. Science. 1985; 229(4718):1104-7. DOI: 10.1126/science.3929379. View

Gibson K, Niederman R . Characterization of two circular satellite species of deoxyribonucleic acid in Rhodopseudomonas spheroides. Arch Biochem Biophys. 1970; 141(2):694-704. DOI: 10.1016/0003-9861(70)90190-6. View

Stein R, Castellvi A, Bogacz J, Wraight C . 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):243-59. DOI: 10.1002/jcb.240240306. View

Michel H, Weyer K, 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; 5(6):1149-58. PMC: 1166921. DOI: 10.1002/j.1460-2075.1986.tb04340.x. View

Brown A, Gilbert C, Guy R, Arntzen C . Triazine herbicide resistance in the photosynthetic bacterium Rhodopseudomonas sphaeroides. Proc Natl Acad Sci U S A. 1984; 81(20):6310-4. PMC: 391913. DOI: 10.1073/pnas.81.20.6310. View

Haworth P, Steinback K . Interaction of Herbicides and Quinone with the Q(B)-Protein of the Diuron-Resistant Chlamydomonas reinhardtii Mutant Dr2. Plant Physiol. 1987; 83(4):1027-31. PMC: 1056495. DOI: 10.1104/pp.83.4.1027. View

Erickson J, Rahire M, Rochaix J, Mets L . Herbicide resistance and cross-resistance: changes at three distinct sites in the herbicide-binding protein. Science. 1985; 228(4696):204-7. DOI: 10.1126/science.228.4696.204. View

Birnboim H, DOLY J . A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979; 7(6):1513-23. PMC: 342324. DOI: 10.1093/nar/7.6.1513. View

Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

10.

Williams J, Steiner L, Feher G, Simon M . Primary structure of the L subunit of the reaction center from Rhodopseudomonas sphaeroides. Proc Natl Acad Sci U S A. 1984; 81(23):7303-7. PMC: 392134. DOI: 10.1073/pnas.81.23.7303. View

11.

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. View

12.

LOWRY O, ROSEBROUGH N, FARR A, RANDALL R . Protein measurement with the Folin phenol reagent. J Biol Chem. 1951; 193(1):265-75. View

13.

Pfister K, Steinback K, Gardner G, Arntzen C . Photoaffinity labeling of an herbicide receptor protein in chloroplast membranes. Proc Natl Acad Sci U S A. 1981; 78(2):981-5. PMC: 319929. DOI: 10.1073/pnas.78.2.981. View

14.

Brown A, Eiserling F, LASCELLES J . Bacteriochlorophyll Synthesis and the Ultrastructure of Wild Type and Mutant Strains of Rhodopseudomonas spheroides. Plant Physiol. 1972; 50(6):743-6. PMC: 366228. DOI: 10.1104/pp.50.6.743. View

15.

Galloway R, Mets L . Atrazine, bromacil, and diuron resistance in chlamydomonas: a single non-mendelian genetic locus controls the structure of the thylakoid binding site. Plant Physiol. 1984; 74(3):469-74. PMC: 1066710. DOI: 10.1104/pp.74.3.469. View

16.

Hirschberg J, McIntosh L . Molecular Basis of Herbicide Resistance in Amaranthus hybridus. Science. 1983; 222(4630):1346-9. DOI: 10.1126/science.222.4630.1346. View