This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
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 Bai, H.
Right arrow Articles by Lu, A-L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bai, H.
Right arrow Articles by Lu, A-L.

 Previous Article  |  Next Article 

Journal of Bacteriology, February 2007, p. 902-910, Vol. 189, No. 3
0021-9193/07/$08.00+0     doi:10.1128/JB.01513-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Physical and Functional Interactions between Escherichia coli MutY Glycosylase and Mismatch Repair Protein MutS{triangledown} ,{dagger}

Haibo Bai and A-Lien Lu*

Department of Biochemistry and Molecular Biology, University of Maryland at Baltimore, Baltimore, Maryland

Received 27 September 2006/ Accepted 9 November 2006

Escherichia coli MutY and MutS increase replication fidelity by removing adenines that were misincorporated opposite 7,8-dihydro-8-oxo-deoxyguanines (8-oxoG), G, or C. MutY DNA glycosylase removes adenines from these mismatches through a short-patch base excision repair pathway and thus prevents G:C-to-T:A and A:T-to-G:C mutations. MutS binds to the mismatches and initiates the long-patch mismatch repair on daughter DNA strands. We have previously reported that the human MutY homolog (hMYH) physically and functionally interacts with the human MutS homolog, hMutS{alpha} (Y. Gu et al., J. Biol. Chem. 277:11135-11142, 2002). Here, we show that a similar relationship between MutY and MutS exists in E. coli. The interaction of MutY and MutS involves the Fe-S domain of MutY and the ATPase domain of MutS. MutS, in eightfold molar excess over MutY, can enhance the binding activity of MutY with an A/8-oxoG mismatch by eightfold. The MutY expression level and activity in mutS mutant strains are sixfold and twofold greater, respectively, than those for the wild-type cells. The frequency of A:T-to-G:C mutations is reduced by two- to threefold in a mutS mutY mutant compared to a mutS mutant. Our results suggest that MutY base excision repair and mismatch repair defend against the mutagenic effect of 8-oxoG lesions in a cooperative manner.


* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, University of Maryland, Baltimore, MD 21201. Phone: (410) 706-4356. Fax: (410) 706-1787. E-mail: aluchang{at}umaryland.edu.

{triangledown} Published ahead of print on 17 November 2006.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.


Journal of Bacteriology, February 2007, p. 902-910, Vol. 189, No. 3
0021-9193/07/$08.00+0     doi:10.1128/JB.01513-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Heinze, R. J., Giron-Monzon, L., Solovyova, A., Elliot, S. L., Geisler, S., Cupples, C. G., Connolly, B. A., Friedhoff, P. (2009). Physical and functional interactions between Escherichia coli MutL and the Vsr repair endonuclease. Nucleic Acids Res 0: gkp380v1-gkp380 [Abstract] [Full Text]  
  • Russo, M. T., De Luca, G., Casorelli, I., Degan, P., Molatore, S., Barone, F., Mazzei, F., Pannellini, T., Musiani, P., Bignami, M. (2009). Role of MUTYH and MSH2 in the Control of Oxidative DNA Damage, Genetic Instability, and Tumorigenesis. Cancer Res. 69: 4372-4379 [Abstract] [Full Text]  
  • Vidales, L. E., Cardenas, L. C., Robleto, E., Yasbin, R. E., Pedraza-Reyes, M. (2009). Defects in the Error Prevention Oxidized Guanine System Potentiate Stationary-Phase Mutagenesis in Bacillus subtilis. J. Bacteriol. 191: 506-513 [Abstract] [Full Text]