Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1991 Oct;173(20):6578–6585. doi: 10.1128/jb.173.20.6578-6585.1991

Frameshift mutations in the bacteriophage Mu repressor gene can confer a trans-dominant virulent phenotype to the phage.

V Geuskens 1, J L Vogel 1, R Grimaud 1, L Desmet 1, N P Higgins 1, A Toussaint 1
PMCID: PMC208995  PMID: 1833383

Abstract

Virulent mutations in the bacteriophage Mu repressor gene were isolated and characterized. Recombination and DNA sequence analysis have revealed that virulence is due to unusual frameshift mutations which change several C-terminal amino acids. The vir mutations are in the same repressor region as the sts amber mutations which, by eliminating several C-terminal amino acids, suppress thermosensitivity of repressor binding to the operators by its N-terminal domain (J. L. Vogel, N. P. Higgins, L. Desmet, V. Geuskens, and A. Toussaint, unpublished data). Vir repressors bind Mu operators very poorly. Thus the Mu repressor C terminus, either by itself or in conjunction with other phage or host proteins, tunes the DNA-binding properties at the repressor N terminus.

Full text

PDF
6578

Images in this article

Selected References

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

  1. Appleyard R K. Segregation of Lambda Lysogenicity during Bacterial Recombination in Escherichia Coli K12. Genetics. 1954 Jul;39(4):429–439. doi: 10.1093/genetics/39.4.429. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bétermier M., Alazard R., Lefrère V., Chandler M. Functional domains of bacteriophage Mu transposase: properties of C-terminal deletions. Mol Microbiol. 1989 Sep;3(9):1159–1171. doi: 10.1111/j.1365-2958.1989.tb00266.x. [DOI] [PubMed] [Google Scholar]
  3. CAMPBELL A. Sensitive mutants of bacteriophage lambda. Virology. 1961 May;14:22–32. doi: 10.1016/0042-6822(61)90128-3. [DOI] [PubMed] [Google Scholar]
  4. Casadaban M. J. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J Mol Biol. 1976 Jul 5;104(3):541–555. doi: 10.1016/0022-2836(76)90119-4. [DOI] [PubMed] [Google Scholar]
  5. Chaconas G., Gloor G., Miller J. L. Amplification and purification of the bacteriophage Mu encoded B transposition protein. J Biol Chem. 1985 Mar 10;260(5):2662–2669. [PubMed] [Google Scholar]
  6. Degnen G. E., Cox E. C. Conditional mutator gene in Escherichia coli: isolation, mapping, and effector studies. J Bacteriol. 1974 Feb;117(2):477–487. doi: 10.1128/jb.117.2.477-487.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Goosen N., van de Putte P. Regulation of Mu transposition. I. Localization of the presumed recognition sites for HimD and Ner functions controlling bacteriophage Mu transcription. Gene. 1984 Oct;30(1-3):41–46. doi: 10.1016/0378-1119(84)90103-3. [DOI] [PubMed] [Google Scholar]
  8. Harrison S. C., Aggarwal A. K. DNA recognition by proteins with the helix-turn-helix motif. Annu Rev Biochem. 1990;59:933–969. doi: 10.1146/annurev.bi.59.070190.004441. [DOI] [PubMed] [Google Scholar]
  9. Higgins N. P., Collier D. A., Kilpatrick M. W., Krause H. M. Supercoiling and integration host factor change the DNA conformation and alter the flow of convergent transcription in phage Mu. J Biol Chem. 1989 Feb 15;264(5):3035–3042. [PubMed] [Google Scholar]
  10. Howe M. M. Prophage deletion mapping of bacteriophage Mu-1. Virology. 1973 Jul;54(1):93–101. doi: 10.1016/0042-6822(73)90118-9. [DOI] [PubMed] [Google Scholar]
  11. Krause H. M., Higgins N. P. On the mu repressor and early DNA intermediates of transposition. Cold Spring Harb Symp Quant Biol. 1984;49:827–834. doi: 10.1101/sqb.1984.049.01.093. [DOI] [PubMed] [Google Scholar]
  12. Krause H. M., Higgins N. P. Positive and negative regulation of the Mu operator by Mu repressor and Escherichia coli integration host factor. J Biol Chem. 1986 Mar 15;261(8):3744–3752. [PubMed] [Google Scholar]
  13. Leach D., Symonds N. The isolation and characterisation of a plaque-forming derivative of bacteriophage Mu carrying a fragment of Tn3 conferring ampicillin resistance. Mol Gen Genet. 1979 May 4;172(2):179–184. doi: 10.1007/BF00268280. [DOI] [PubMed] [Google Scholar]
  14. Leung P. C., Teplow D. B., Harshey R. M. Interaction of distinct domains in Mu transposase with Mu DNA ends and an internal transpositional enhancer. Nature. 1989 Apr 20;338(6217):656–658. doi: 10.1038/338656a0. [DOI] [PubMed] [Google Scholar]
  15. Pakula A. A., Sauer R. T. Genetic analysis of protein stability and function. Annu Rev Genet. 1989;23:289–310. doi: 10.1146/annurev.ge.23.120189.001445. [DOI] [PubMed] [Google Scholar]
  16. Picard D., Salser S. J., Yamamoto K. R. A movable and regulable inactivation function within the steroid binding domain of the glucocorticoid receptor. Cell. 1988 Sep 23;54(7):1073–1080. doi: 10.1016/0092-8674(88)90122-5. [DOI] [PubMed] [Google Scholar]
  17. Résibois A., Toussaint A., van Gijsegem F., Faelen M. Physical characterization of mini-mu and mini-D108. Gene. 1981 Jun-Jul;14(1-2):103–113. doi: 10.1016/0378-1119(81)90152-9. [DOI] [PubMed] [Google Scholar]
  18. Simons R. W., Houman F., Kleckner N. Improved single and multicopy lac-based cloning vectors for protein and operon fusions. Gene. 1987;53(1):85–96. doi: 10.1016/0378-1119(87)90095-3. [DOI] [PubMed] [Google Scholar]
  19. TAYLOR A. L. BACTERIOPHAGE-INDUCED MUTATION IN ESCHERICHIA COLI. Proc Natl Acad Sci U S A. 1963 Dec;50:1043–1051. doi: 10.1073/pnas.50.6.1043. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Vogel J. L., Li Z. J., Howe M. M., Toussaint A., Higgins N. P. Temperature-sensitive mutations in the bacteriophage Mu c repressor locate a 63-amino-acid DNA-binding domain. J Bacteriol. 1991 Oct;173(20):6568–6577. doi: 10.1128/jb.173.20.6568-6577.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene. 1985;33(1):103–119. doi: 10.1016/0378-1119(85)90120-9. [DOI] [PubMed] [Google Scholar]

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

RESOURCES