Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1997 May;179(9):3073–3075. doi: 10.1128/jb.179.9.3073-3075.1997

The integration host factor-DNA complex upstream of the early promoter of bacteriophage Mu is functionally symmetric.

P van Ulsen 1, M Hillebrand 1, L Zulianello 1, P van de Putte 1, N Goosen 1
PMCID: PMC179079  PMID: 9139933

Abstract

Inversion of the ihf site in the promoter region of the early promoter of bacteriophage Mu did not influence the integration host factor (IHF)-mediated functions. IHF bound to this inverted site could counteract H-NS-mediated repression, directly activate transcription, and support lytic growth of bacteriophage Mu. This implies that the IHF heterodimer and its asymmetrical binding site form a functionally symmetrical complex.

Full Text

The Full Text of this article is available as a PDF (110.1 KB).

Selected References

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

  1. Friedman D. I. Integration host factor: a protein for all reasons. Cell. 1988 Nov 18;55(4):545–554. doi: 10.1016/0092-8674(88)90213-9. [DOI] [PubMed] [Google Scholar]
  2. Giladi H., Gottesman M., Oppenheim A. B. Integration host factor stimulates the phage lambda pL promoter. J Mol Biol. 1990 May 5;213(1):109–121. doi: 10.1016/S0022-2836(05)80124-X. [DOI] [PubMed] [Google Scholar]
  3. Giladi H., Igarashi K., Ishihama A., Oppenheim A. B. Stimulation of the phage lambda pL promoter by integration host factor requires the carboxy terminus of the alpha-subunit of RNA polymerase. J Mol Biol. 1992 Oct 20;227(4):985–990. doi: 10.1016/0022-2836(92)90514-k. [DOI] [PubMed] [Google Scholar]
  4. Giladi H., Koby S., Gottesman M. E., Oppenheim A. B. Supercoiling, integration host factor, and a dual promoter system, participate in the control of the bacteriophage lambda pL promoter. J Mol Biol. 1992 Apr 20;224(4):937–948. doi: 10.1016/0022-2836(92)90461-r. [DOI] [PubMed] [Google Scholar]
  5. Giladi H., Murakami K., Ishihama A., Oppenheim A. B. Identification of an UP element within the IHF binding site at the PL1-PL2 tandem promoter of bacteriophage lambda. J Mol Biol. 1996 Jul 26;260(4):484–491. doi: 10.1006/jmbi.1996.0416. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. Goosen N., van de Putte P. Role of ner protein in bacteriophage Mu transposition. J Bacteriol. 1986 Aug;167(2):503–507. doi: 10.1128/jb.167.2.503-507.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Goosen N., van de Putte P. The regulation of transcription initiation by integration host factor. Mol Microbiol. 1995 Apr;16(1):1–7. doi: 10.1111/j.1365-2958.1995.tb02386.x. [DOI] [PubMed] [Google Scholar]
  9. Granston A. E., Nash H. A. Characterization of a set of integration host factor mutants deficient for DNA binding. J Mol Biol. 1993 Nov 5;234(1):45–59. doi: 10.1006/jmbi.1993.1562. [DOI] [PubMed] [Google Scholar]
  10. Hoover T. R., Santero E., Porter S., Kustu S. The integration host factor stimulates interaction of RNA polymerase with NIFA, the transcriptional activator for nitrogen fixation operons. Cell. 1990 Oct 5;63(1):11–22. doi: 10.1016/0092-8674(90)90284-l. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. Lee E. C., Hales L. M., Gumport R. I., Gardner J. F. The isolation and characterization of mutants of the integration host factor (IHF) of Escherichia coli with altered, expanded DNA-binding specificities. EMBO J. 1992 Jan;11(1):305–313. doi: 10.1002/j.1460-2075.1992.tb05053.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Mengeritsky G., Goldenberg D., Mendelson I., Giladi H., Oppenheim A. B. Genetic and biochemical analysis of the integration host factor of Escherichia coli. J Mol Biol. 1993 Jun 5;231(3):646–657. doi: 10.1006/jmbi.1993.1316. [DOI] [PubMed] [Google Scholar]
  14. Nunes-Düby S. E., Smith-Mungo L. I., Landy A. Single base-pair precision and structural rigidity in a small IHF-induced DNA loop. J Mol Biol. 1995 Oct 20;253(2):228–242. doi: 10.1006/jmbi.1995.0548. [DOI] [PubMed] [Google Scholar]
  15. Pagel J. M., Hatfield G. W. Integration host factor-mediated expression of the ilvGMEDA operon of Escherichia coli. J Biol Chem. 1991 Jan 25;266(3):1985–1996. [PubMed] [Google Scholar]
  16. Schmid M. B. More than just "histone-like" proteins. Cell. 1990 Nov 2;63(3):451–453. doi: 10.1016/0092-8674(90)90438-k. [DOI] [PubMed] [Google Scholar]
  17. Surette M. G., Chaconas G. A protein factor which reduces the negative supercoiling requirement in the Mu DNA strand transfer reaction is Escherichia coli integration host factor. J Biol Chem. 1989 Feb 15;264(5):3028–3034. [PubMed] [Google Scholar]
  18. Tanaka I., Appelt K., Dijk J., White S. W., Wilson K. S. 3-A resolution structure of a protein with histone-like properties in prokaryotes. Nature. 1984 Aug 2;310(5976):376–381. doi: 10.1038/310376a0. [DOI] [PubMed] [Google Scholar]
  19. Werner M. H., Clore G. M., Gronenborn A. M., Nash H. A. Symmetry and asymmetry in the function of Escherichia coli integration host factor: implications for target identification by DNA-binding proteins. Curr Biol. 1994 Jun 1;4(6):477–487. doi: 10.1016/s0960-9822(00)00108-1. [DOI] [PubMed] [Google Scholar]
  20. Yang C. C., Nash H. A. The interaction of E. coli IHF protein with its specific binding sites. Cell. 1989 Jun 2;57(5):869–880. doi: 10.1016/0092-8674(89)90801-5. [DOI] [PubMed] [Google Scholar]
  21. Yang S. W., Nash H. A. Specific photocrosslinking of DNA-protein complexes: identification of contacts between integration host factor and its target DNA. Proc Natl Acad Sci U S A. 1994 Dec 6;91(25):12183–12187. doi: 10.1073/pnas.91.25.12183. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Zulianello L., de la Gorgue de Rosny E., van Ulsen P., van de Putte P., Goosen N. The HimA and HimD subunits of integration host factor can specifically bind to DNA as homodimers. EMBO J. 1994 Apr 1;13(7):1534–1540. doi: 10.1002/j.1460-2075.1994.tb06415.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Zulianello L., van Ulsen P., van de Putte P., Goosen N. Participation of the flank regions of the integration host factor protein in the specificity and stability of DNA binding. J Biol Chem. 1995 Jul 28;270(30):17902–17907. doi: 10.1074/jbc.270.30.17902. [DOI] [PubMed] [Google Scholar]
  24. van Rijn P. A., Goosen N., Turk S. C., van de Putte P. Regulation of phage Mu repressor transcription by IHF depends on the level of the early transcription. Nucleic Acids Res. 1989 Dec 25;17(24):10203–10212. doi: 10.1093/nar/17.24.10203. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. van Rijn P. A., Goosen N., van de Putte P. Integration host factor of Escherichia coli regulates early- and repressor transcription of bacteriophage Mu by two different mechanisms. Nucleic Acids Res. 1988 May 25;16(10):4595–4605. doi: 10.1093/nar/16.10.4595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. van Ulsen P., Hillebrand M., Kainz M., Collard R., Zulianello L., van de Putte P., Gourse R. L., Goosen N. Function of the C-terminal domain of the alpha subunit of Escherichia coli RNA polymerase in basal expression and integration host factor-mediated activation of the early promoter of bacteriophage Mu. J Bacteriol. 1997 Jan;179(2):530–537. doi: 10.1128/jb.179.2.530-537.1997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. van Ulsen P., Hillebrand M., Zulianello L., van de Putte P., Goosen N. Integration host factor alleviates the H-NS-mediated repression of the early promoter of bacteriophage Mu. Mol Microbiol. 1996 Aug;21(3):567–578. doi: 10.1111/j.1365-2958.1996.tb02565.x. [DOI] [PubMed] [Google Scholar]

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

RESOURCES