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 Lombardo, M.-J.
Right arrow Articles by Rosenberg, S. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lombardo, M.-J.
Right arrow Articles by Rosenberg, S. M.

 Previous Article  |  Next Article 

Journal of Bacteriology, November 2000, p. 6287-6291, Vol. 182, No. 22
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

radC102 of Escherichia coli Is an Allele of recG

Mary-Jane Lombardo* and Susan M. Rosenberg

Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030

Received 22 May 2000/Accepted 21 August 2000

The radC102 mutation causes mild UV and X-ray sensitivity and was mapped previously to near pyrE and recG at 82 min on the Escherichia coli chromosome (I. Felzenszwalb, N. J. Sargentini, and K. C. Smith, Radiat. Res. 97:615-625, 1984). We report that radC102 has two striking phenotypes characteristic of recG mutations. First, it causes dramatically increased RecA-dependent mutation in a stationary-phase mutation assay. Second, it causes extreme UV sensitivity in combination with ruv mutations affecting the RuvABC Holliday junction resolution system. DNA sequencing of the radC and recG genes in radC102 strains revealed that the radC102 mutation creates a stop codon in recG that is predicted to truncate the RecG protein at 410 of 603 amino acids. A low-copy-number plasmid carrying the radC+ gene did not affect the UV sensitivity of a wild-type strain, a radC102 strain, or a recG258::Tn10mini-kan strain. We conclude that radC102 is an allele of recG and that the function of the RadC protein remains to be determined.

* Corresponding author. Mailing address: Department of Molecular and Human Genetics, Baylor College of Medicine, One Baylor Plaza, Room S809, Mail Stop 225, Houston, TX 77030-3498. Phone: (713) 798-6693. Fax: (713) 798-8704. E-mail: lombardo{at}bcm.tmc.edu.

Journal of Bacteriology, November 2000, p. 6287-6291, Vol. 182, No. 22
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Attaiech, L., Granadel, C., Claverys, J.-P., Martin, B. (2008). RadC, a Misleading Name?. J. Bacteriol. 190: 5729-5732 [Abstract] [Full Text]  
  • Ruiz-Maso, J. A., Anand, S. P., Espinosa, M., Khan, S. A., del Solar, G. (2006). Genetic and Biochemical Characterization of the Streptococcus pneumoniae PcrA Helicase and Its Role in Plasmid Rolling Circle Replication. J. Bacteriol. 188: 7416-7425 [Abstract] [Full Text]  
  • Donaldson, J. R., Courcelle, C. T., Courcelle, J. (2004). RuvAB and RecG Are Not Essential for the Recovery of DNA Synthesis Following UV-Induced DNA Damage in Escherichia coli. Genetics 166: 1631-1640 [Abstract] [Full Text]  
  • McGlynn, P., Lloyd, R. G. (2001). Action of RuvAB at Replication Fork Structures. J. Biol. Chem. 276: 41938-41944 [Abstract] [Full Text]  
  • Bull, H. J., Lombardo, M.-J., Rosenberg, S. M. (2001). Stationary-phase mutation in the bacterial chromosome: Recombination protein and DNA polymerase IV dependence. Proc. Natl. Acad. Sci. USA 98: 8334-8341 [Abstract] [Full Text]  
  • Avison, M. B., Horton, R. E., Walsh, T. R., Bennett, P. M. (2001). Escherichia coli CreBC Is a Global Regulator of Gene Expression That Responds to Growth in Minimal Media. J. Biol. Chem. 276: 26955-26961 [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»