Hostname: page-component-5cf477f64f-mgq6s Total loading time: 0 Render date: 2025-04-03T05:00:08.922Z Has data issue: false hasContentIssue false
  • English
  • Français

Deoxyribonuclease-deficient mutants of Ustilago maydis with altered recombination frequencies

Published online by Cambridge University Press:  14 April 2009

Rosemary Badman
Rosemary Badman
Affiliation:
National Institute for Medical Research, Mill Hill, London NW7 1AA
Rights & Permissions [Opens in a new window]

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Current molecular models of genetic recombination invoke steps mediated by deoxyribonucleases. It is likely therefore that some mutants deficient in these enzymes would have defective recombination mechnisms. Mutants of Ustilago maydis deficient in extracellular and intracellular DNase activity have been isolated. Three of the extracellular mutants are recessive and non-complementing, as are four of the intracellular mutants. The loci for extracellular and intracellular DNase deficiency have been named nuc-1 and nuc-2 respectively, and they are linked.

In crosses where each parent was deficient in both extracellular and intracellular DNase activity, meiotic allelic recombination (gene conversion) within the nar locus was abolished, although crossing-over in one tested interval was apparently normal in frequency. In DNase-deficient diploids, no mitotic allelic recombination in the nar locus was observed and the distribution of crossing over was abnormal. Nuclease deficiency did not appear to have any strong effect on radiation sensitivity.

Type
Research Article
Information
Genetics Research , Volume 20 , Issue 2 , October 1972 , pp. 213 - 229
Copyright
Copyright © Cambridge University Press 1972

References

REFERENCES

Alberts, B. M., Amodio, F. S., Jenkins, M., Gutmann, E. D. & Ferris, F. L. (1968). DNA cellulose chromatography. Cold Spring Harbor Symposium of Quantitative Biology 33, 289–305.CrossRefGoogle ScholarPubMed
Badman, R. (1971). Ph.D. Thesis, National Institute for Medical Research, London, N.W. 7.Google Scholar
Bray, G. (1960). A simple efficient liquid scintillator for counting aqueous solutions in a liquid scintillation counter. Analytical Biochemistry 1, 279–285.CrossRefGoogle Scholar
Buttin, G. & Wright, M. R. (1968). Enzymatic DNA degradation in E, coli: its relationship to the synthetic processes at the chromosome level. Cold Spring Harbor Symposium of Quantitative Biology 33, 259–269.CrossRefGoogle Scholar
Catcheside, D. G. & Austin, B. (1971). Common regulation of recombination at the amination-1 and histidine-2 loci in Neurospora crassa. Australian Journal of Biological Sciences 24, 107–115CrossRefGoogle ScholarPubMed
Davern, C. I. (1971). Molecular aspects of genetic recombination. Progress in Nucleic Acid Research and Molecular Biology 11, 229–252.CrossRefGoogle ScholarPubMed
Fincham, J. R. S. & Holliday, R. (1970). An explanation of fine structure map expansion in terms of excision repair. Molecular and General Genetics 109, 309–322.CrossRefGoogle ScholarPubMed
Fogel, S. & Mortimer, R. K. (1969). Informational transfer in meiotic gene conversion. Proceedings of the National Academy of Sciences, U.S.A. 62, 92–103.CrossRefGoogle ScholarPubMed
Fortuin, J. J. H. (1971). Another two genes controlling mitotic intragenic recombination and recovery from UV damage in Aspergillus nidulans. II. Recombination behaviour and X-ray sensitivity of uvs D and uvs E mutants. Mutation Research 11, 265–277.Google Scholar
Holliday, R. (1961 a). The genetics of Ustilago maydis. Genetical Research 2, 204–230.CrossRefGoogle Scholar
Holliday, R. (1961 b). Induced mitotic crossing over in Ustilago maydis. Genetical Research 2, 231–248.CrossRefGoogle Scholar
Holliday, R. (1964). A mechanism for gene conversion in fungi. Genetical Research 5, 284–304.CrossRefGoogle Scholar
Holliday, R. (1966). Studies on mitotic gene conversion in Ustilago. Genetical Research 8, 323–337.CrossRefGoogle ScholarPubMed
Holliday, R. (1967). Altered recombination frequencies in radiation-sensitive strains of Ustilago. Mutation Research 4, 275–288.CrossRefGoogle Scholar
Holliday, R. (1968). Genetic recombination in fungi. In Replication and Recombination of Genetic Material, pp. 157–174.Australian Academy of Science.Google Scholar
Holliday, R. & Halliwell, R. (1968). An endonuclease-deficient strain of Ustilago maydis. Genetical Research 12, 95–98.CrossRefGoogle ScholarPubMed
Howard-Flanders, P. (1968). DNA repair. Annual Review of Biochemistry 37, 175–200.CrossRefGoogle ScholarPubMed
Hunnable, E. G. & Cox, B. S. (1971). The genetic control of dark recombination in yeast. Mutation Research 13, 297–309.CrossRefGoogle Scholar
Ishikawa, T., Toh-E, A., Ono, I. & Hasunuma, K. (1969). Isolation and characterisation of nuclease mutants in Neurospora crassa. Genetics 63, 75–92.CrossRefGoogle ScholarPubMed
Lea, D. E. & Coulson, C. A. (1949). The distribution of the numbers of mutants in bacterial populations. Journal of Genetics 49, 264–285.CrossRefGoogle ScholarPubMed
Lewis, D. (1961). Genetical analysis of methionine suppressors in Coprinus. Genetical Research 2, 141–155.CrossRefGoogle Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. & Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193, 265–275.CrossRefGoogle ScholarPubMed
Morgan, D. H. (1966). Suppression of ‘purple’ in Coprinus lagopus – an anomalous genetic situation. Genetical Research 7, 195–206.CrossRefGoogle Scholar
Puhalla, J. E. (1968). Compatibility reactions on solid medium and interstrain inhibition in Ustilago maydis. Genetics 60, 461–474.CrossRefGoogle ScholarPubMed
Radding, C. M. (1970). The role of exonuclease and β protein of bacteriophage A in genetic recombination. I. Effects of red mutants on protein structure. Journal of Molecular Biology 52, 491–499.CrossRefGoogle ScholarPubMed
Richardson, C. C. (1969). Enzymes in DNA metabolism. Annual Review of Biochemistry 38, 795–840.CrossRefGoogle ScholarPubMed
Rodarte-Ramón, U. S. & Mortimer, R. K. (1972). Radiation-induced recombination in Saccharomyces: isolation and genetic study of recombination-deficient mutants. Radiation Research 49, 133–147.CrossRefGoogle ScholarPubMed
Schroeder, A. L. (1970). UV-sensitive mutants of Neurospora. Molecular and General Genetics 107, 291–304.CrossRefGoogle Scholar
Strauss, B. & Marone, R. (1967). A heat-labile inhibitor of deoxyribonucleic acid degradation in Bacillus subtilis. Biochemical and Biophysical Research Communications 29, 143–147.CrossRefGoogle ScholarPubMed
Unrau, P. & Holliday, R. (1972). Recombination during blocked chromosome replication in temperature-sensitive strains of Ustilago maydis. Genetical Research (in the Press.)CrossRefGoogle Scholar
Whitehouse, H. L. K. (1963). A theory of crossing over by means of hybrid deoxyribonucleic acid. Nature 199, 1034–1040.CrossRefGoogle ScholarPubMed
Willetts, N. C. & Clark, A. J. (1969). Characteristics of some multiply recombination deficient strains of Escherichia coli. Journal of Bacteriology 100, 231–239.CrossRefGoogle ScholarPubMed