Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1989 Mar;171(3):1284–1287. doi: 10.1128/jb.171.3.1284-1287.1989

Molybdenum accumulation in chlD mutants of Escherichia coli.

D Scott 1, N K Amy 1
PMCID: PMC209742  PMID: 2646274

Abstract

The content of molybdenum in wild-type and chlD cells was measured under a variety of growth conditions to determine if cells with a defective chlD gene were able to accumulate molybdenum. The chlD cells accumulated less molybdenum than wild-type cells did but concentrated molybdenum to a level at least 20-fold higher than the concentration in the culture medium. Molybdenum was present within spheroplasts of chlD cells and was not dialyzable. The chlD cells accumulated as much molybdenum as wild-type cells did when grown in medium containing 0.1 mM molybdate; thus, the capability of incorporation of molybdenum into cellular component(s) was equivalent to that of the wild type under these conditions.

Full text

PDF
1284

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Amy N. K. Identification of the molybdenum cofactor in chlorate-resistant mutants of Escherichia coli. J Bacteriol. 1981 Oct;148(1):274–282. doi: 10.1128/jb.148.1.274-282.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Amy N. K., Rajagopalan K. V. Characterization of molybdenum cofactor from Escherichia coli. J Bacteriol. 1979 Oct;140(1):114–124. doi: 10.1128/jb.140.1.114-124.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Campbell A. M., del Campillo-Campbell A., Villaret D. B. Molybdate reduction by Escherichia coli K-12 and its chl mutants. Proc Natl Acad Sci U S A. 1985 Jan;82(1):227–231. doi: 10.1073/pnas.82.1.227. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cardenas J., Mortenson L. E. Determination of molybdenum and tungsten in biological materials. Anal Biochem. 1974 Aug;60(2):372–381. doi: 10.1016/0003-2697(74)90244-9. [DOI] [PubMed] [Google Scholar]
  5. Giordano G., Saracino L., Grillet L. Identification in various chlorate-resistant mutants of a protein involved in the activation of nitrate reductase in the soluble fraction of a chlA mutant of Escherichia coli K-12. Biochim Biophys Acta. 1985 Apr 17;839(2):181–190. doi: 10.1016/0304-4165(85)90035-2. [DOI] [PubMed] [Google Scholar]
  6. Glaser J. H., DeMoss J. A. Phenotypic restoration by molybdate of nitrate reductase activity in chlD mutants of Escherichia coli. J Bacteriol. 1971 Nov;108(2):854–860. doi: 10.1128/jb.108.2.854-860.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Imperial J., Ugalde R. A., Shah V. K., Brill W. J. Mol- mutants of Klebsiella pneumoniae requiring high levels of molybdate for nitrogenase activity. J Bacteriol. 1985 Sep;163(3):1285–1287. doi: 10.1128/jb.163.3.1285-1287.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Iuchi S., Lin E. C. Molybdenum effector of fumarate reductase repression and nitrate reductase induction in Escherichia coli. J Bacteriol. 1987 Aug;169(8):3720–3725. doi: 10.1128/jb.169.8.3720-3725.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Johann S., Hinton S. M. Cloning and nucleotide sequence of the chlD locus. J Bacteriol. 1987 May;169(5):1911–1916. doi: 10.1128/jb.169.5.1911-1916.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Miller J. B., Amy N. K. Molybdenum cofactor in chlorate-resistant and nitrate reductase-deficient insertion mutants of Escherichia coli. J Bacteriol. 1983 Aug;155(2):793–801. doi: 10.1128/jb.155.2.793-801.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Miller J. B., Scott D. J., Amy N. K. Molybdenum-sensitive transcriptional regulation of the chlD locus of Escherichia coli. J Bacteriol. 1987 May;169(5):1853–1860. doi: 10.1128/jb.169.5.1853-1860.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Pascal M. C., Burini J. F., Ratouchniak J., Chippaux M. Regulation of the nitrate reductase operon: effect of mutations in chlA, B, D and E genes. Mol Gen Genet. 1982;188(1):103–106. doi: 10.1007/BF00333001. [DOI] [PubMed] [Google Scholar]
  13. Showe M. K., DeMoss J. A. Localization and regulation of synthesis of nitrate reductase in Escherichia coli. J Bacteriol. 1968 Apr;95(4):1305–1313. doi: 10.1128/jb.95.4.1305-1313.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Sperl G. T., DeMoss J. A. chlD gene function in molybdate activation of nitrate reductase. J Bacteriol. 1975 Jun;122(3):1230–1238. doi: 10.1128/jb.122.3.1230-1238.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Ugalde R. A., Imperial J., Shah V. K., Brill W. J. Biosynthesis of the iron-molybdenum cofactor and the molybdenum cofactor in Klebsiella pneumoniae: effect of sulfur source. J Bacteriol. 1985 Dec;164(3):1081–1087. doi: 10.1128/jb.164.3.1081-1087.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Viñuela E., Algranati I. D., Ochoa S. Synthesis of virus-specific proteins in Escherichia coli infected with the RNA bacteriophage MS2. Eur J Biochem. 1967 Mar;1(1):3–11. doi: 10.1007/978-3-662-25813-2_2. [DOI] [PubMed] [Google Scholar]
  17. Weiss R. L. Protoplast formation in Escherichia coli. J Bacteriol. 1976 Nov;128(2):668–670. doi: 10.1128/jb.128.2.668-670.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. del Campillo-Campbell A., Campbell A. Molybdenum cofactor requirement for biotin sulfoxide reduction in Escherichia coli. J Bacteriol. 1982 Feb;149(2):469–478. doi: 10.1128/jb.149.2.469-478.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES