Abstract
Transformation was used to perform ratio test crosses with mutant strains of Azotobacter vinelandii unable to fix N2. Mutations that simultaneously eliminated both components of nitrogenase (nif-1 and nif-2) were tightly linked. The nif-45 mutation that resulted in the absence of an active molybdenum cofactor was closer to nif-1 and nif-2 than to any of the other nif mutations. Strains that lacked component I carried mutations that were closely linked to each other. Mutations that probably were located in the structural genes for components I and II appeared to be relatively close to each other on the A. vinelandii genome.
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Selected References
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- Brill W. J., Westphal J., Stieghorst M., Davis L. C., Shah V. K. Detection of nitrogenase components and other nonheme iron proteins in polyacrylamide gels. Anal Biochem. 1974 Jul;60(1):237–241. doi: 10.1016/0003-2697(74)90149-3. [DOI] [PubMed] [Google Scholar]
- DE WITT C. W., ROWE J. A. N,O-Diacetylneuraminic acid and N-acetylneuraminic acid in Escherichia coli. Nature. 1959 Aug 1;184(Suppl 6):381–382. doi: 10.1038/184381b0. [DOI] [PubMed] [Google Scholar]
- Nagatani H. H., Shah V. K., Brill W. J. Activation of inactive nitrogenase by acid-treated component I. J Bacteriol. 1974 Nov;120(2):697–701. doi: 10.1128/jb.120.2.697-701.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Page W. J., Sadoff H. L. Physiological factors affecting transformation of Azotobacter vinelandii. J Bacteriol. 1976 Mar;125(3):1080–1087. doi: 10.1128/jb.125.3.1080-1087.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shah V. K., Davis I. C., Gordon J. K., Orme-Johnson W. H., Brill W. J. Nitrogenase. 3. Nitrogenaseless mutants of Azotobacter vinelandii: activities, cross-reactions and EPR spectra. Biochim Biophys Acta. 1973 Jan 18;292(1):246–255. doi: 10.1016/0005-2728(73)90269-7. [DOI] [PubMed] [Google Scholar]
- Shah V. K., Davis L. C., Stieghorst M., Brill W. J. Mutant of Azotobacter vinelandii that hyperproduces nitrogenase component II. J Bacteriol. 1974 Feb;117(2):917–919. doi: 10.1128/jb.117.2.917-919.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- St John R. T., Johnston H. M., Seidman C., Garfinkel D., Gordon J. K., Shah V. K., Brill W. J. Biochemistry and genetics of Klebsiella pneumoniae mutant strains unable to fix N2. J Bacteriol. 1975 Mar;121(3):759–765. doi: 10.1128/jb.121.3.759-765.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Strandberg G. W., Wilson P. W. Formation of the nitrogen-fixing enzyme system in Azotobacter vinelandii. Can J Microbiol. 1968 Jan;14(1):25–31. doi: 10.1139/m68-005. [DOI] [PubMed] [Google Scholar]
- Streicher S., Gurney E., Valentine R. C. Transduction of the nitrogen-fixation genes in Klebsiella pneumoniae. Proc Natl Acad Sci U S A. 1971 Jun;68(6):1174–1177. doi: 10.1073/pnas.68.6.1174. [DOI] [PMC free article] [PubMed] [Google Scholar]