This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Li, S.
Right arrow Articles by Waters, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Li, S.
Right arrow Articles by Waters, R.

 Previous Article  |  Next Article 

Journal of Bacteriology, August 1998, p. 3750-3756, Vol. 180, No. 15
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Escherichia coli Strains Lacking Protein HU Are UV Sensitive due to a Role for HU in Homologous Recombination

Shisheng Li and Raymond Waters*

School of Biological Sciences, University of Wales Swansea, Swansea SA2 8PP, United Kingdom

Received 13 June 1997/Accepted 15 May 1998

hupA and hupB encode the alpha  and beta  subunits of the Escherichia coli histone-like protein HU. Here we show that E. coli hup mutants are sensitive to UV in the rec+ sbc+, recBC sbcA, recBC sbcBC, umuDC, recF, and recD backgrounds. However, hupAB mutations do not enhance the UV sensitivity of resolvase-deficient recG ruvA strains. hupAB uvrA and hupAB recG strains are supersensitive to UV. hup mutations enhance the UV sensitivity of ruvA strains to a much lesser extent but enhance that of rus-1 ruvA strains to the same extent as for rus+ ruv+ strains. Our results suggest that HU plays a role in recombinational DNA repair that is not specifically limited to double-strand break repair or daughter strand gap repair; the lack of HU affects the RecG RusA and RuvABC pathways for Holliday junction processing equally if the two pathways are equally active in recombinational repair; the function of HU is not in the substrate processing step or in the RecFOR-directed synapsis action during recombinational repair. Furthermore, the UV sensitivity of hup mutants cannot be suppressed by overexpression of wild-type or mutant gyrB, which confers novobiocin resistance, or by different concentrations of a gyrase inhibitor that can increase or decrease the supercoiling of chromosomal DNA.

* Corresponding author. Mailing address: School of Biological Sciences, University of Wales Swansea, Singleton Park, Swansea SA2 8PP, United Kingdom. Phone: (44) 1792 295384. Fax: (44) 1792 295447. E-mail: r.waters{at}swansea.ac.uk.

Journal of Bacteriology, August 1998, p. 3750-3756, Vol. 180, No. 15
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Pohjoismaki, J. L. O., Goffart, S., Tyynismaa, H., Willcox, S., Ide, T., Kang, D., Suomalainen, A., Karhunen, P. J., Griffith, J. D., Holt, I. J., Jacobs, H. T. (2009). Human Heart Mitochondrial DNA Is Organized in Complex Catenated Networks Containing Abundant Four-way Junctions and Replication Forks. J. Biol. Chem. 284: 21446-21457 [Abstract] [Full Text]  
  • Kamashev, D., Balandina, A., Mazur, A. K., Arimondo, P. B., Rouviere-Yaniv, J. (2008). HU binds and folds single-stranded DNA. Nucleic Acids Res 36: 1026-1036 [Abstract] [Full Text]  
  • Kow, Y. W., Imhoff, B., Weiss, B., Hung, D. C. I., Hindoyan, A. A., Story, R. M., Goodman, S. D. (2007). Escherichia coli HU protein has a role in the repair of abasic sites in DNA. Nucleic Acids Res 35: 6672-6680 [Abstract] [Full Text]  
  • Williams, A. B., Foster, P. L. (2007). The Escherichia coli Histone-like Protein HU Has a Role in Stationary Phase Adaptive Mutation. Genetics 177: 723-735 [Abstract] [Full Text]  
  • Pohjoismaki, J. L. O., Wanrooij, S., Hyvarinen, A. K., Goffart, S., Holt, I. J., Spelbrink, J. N., Jacobs, H. T. (2006). Alterations to the expression level of mitochondrial transcription factor A, TFAM, modify the mode of mitochondrial DNA replication in cultured human cells. Nucleic Acids Res 34: 5815-5828 [Abstract] [Full Text]  
  • Robbins-Manke, J. L., Zdraveski, Z. Z., Marinus, M., Essigmann, J. M. (2005). Analysis of Global Gene Expression and Double-Strand-Break Formation in DNA Adenine Methyltransferase- and Mismatch Repair-Deficient Escherichia coli. J. Bacteriol. 187: 7027-7037 [Abstract] [Full Text]  
  • Sand, O., Gingras, M., Beck, N., Hall, C., Trun, N. (2003). Phenotypic characterization of overexpression or deletion of the Escherichia coli crcA, cspE and crcB genes. Microbiology 149: 2107-2117 [Abstract] [Full Text]  
  • Hashimoto, M., Imhoff, B., Ali, M. M., Kow, Y. W. (2003). HU Protein of Escherichia coli Has a Role in the Repair of Closely Opposed Lesions in DNA. J. Biol. Chem. 278: 28501-28507 [Abstract] [Full Text]  
  • Balandina, A., Kamashev, D., Rouviere-Yaniv, J. (2002). The Bacterial Histone-like Protein HU Specifically Recognizes Similar Structures in All Nucleic Acids. DNA, RNA, AND THEIR HYBRIDS. J. Biol. Chem. 277: 27622-27628 [Abstract] [Full Text]  
  • Kar, S., Adhya, S. (2001). Recruitment of HU by piggyback: a special role of GalR in repressosome assembly. Genes Dev. 15: 2273-2281 [Abstract] [Full Text]  
  • Ross, M. A., Setlow, P. (2000). The Bacillus subtilis HBsu Protein Modifies the Effects of alpha /beta -Type, Small Acid-Soluble Spore Proteins on DNA. J. Bacteriol. 182: 1942-1948 [Abstract] [Full Text]  
  • Joux, F., Jeffrey, W. H., Lebaron, P., Mitchell, D. L. (1999). Marine Bacterial Isolates Display Diverse Responses to UV-B Radiation. Appl. Environ. Microbiol. 65: 3820-3827 [Abstract] [Full Text]  
  • Bartels, F., Fernandez, S., Holtel, A., Timmis, K. N., de Lorenzo, V. (2001). The Essential HupB and HupN Proteins of Pseudomonas putida Provide Redundant and Nonspecific DNA-bending Functions. J. Biol. Chem. 276: 16641-16648 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»