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 Rajman, L. A.
Right arrow Articles by Lovett, S. T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Rajman, L. A.
Right arrow Articles by Lovett, S. T.

 Previous Article  |  Next Article 

Journal of Bacteriology, February 2000, p. 607-612, Vol. 182, No. 3
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

A Thermostable Single-Strand DNase from Methanococcus jannaschii Related to the RecJ Recombination and Repair Exonuclease from Escherichia coli

Luis A. Rajman and Susan T. Lovett*

Department of Biology and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02454-9110

Received 7 September 1999/Accepted 5 November 1999

The RecJ protein of Escherichia coli plays an important role in a number of DNA repair and recombination pathways. RecJ catalyzes processive degradation of single-stranded DNA in a 5'-to-3' direction. Sequences highly related to those encoding RecJ can be found in most of the eubacterial genomes sequenced to date. From alignment of these sequences, seven conserved motifs are apparent. At least five of these motifs are shared among a large family of proteins in eubacteria, eukaryotes, and archaea, including the PPX1 polyphosphatase of yeast and Drosophila Prune. Archaeal genomes are particularly rich in such sequences, but it has not been clear whether any of the encoded proteins play a functional role similar to that of RecJ exonuclease. We have investigated three such proteins from Methanococcus jannaschii with the strongest overall sequence similarity to E. coli RecJ. Two of the genes, MJ0977 and MJ0831, partially complement a recJ mutant phenotype in E. coli. The expression of MJ0977 in E. coli resulted in high levels of a thermostable single-stranded DNase activity with properties similar to those of RecJ exonuclease. Despite overall weak sequence similarity between the MJ0977 product and RecJ, these nucleases are likely to have similar biological functions.

* Corresponding author. Mailing address: Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02454-9110. Phone: (781) 736-2487. Fax: (781) 736-2405. E-mail: lovett{at}hydra.rose.brandeis.edu.

Journal of Bacteriology, February 2000, p. 607-612, Vol. 182, No. 3
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Kickstein, E., Harms, K., Wackernagel, W. (2007). Deletions of recBCD or recD influence genetic transformation differently and are lethal together with a recJ deletion in Acinetobacter baylyi. Microbiology 153: 2259-2270 [Abstract] [Full Text]  
  • Han, E. S., Cooper, D. L., Persky, N. S., Sutera, V. A. Jr, Whitaker, R. D., Montello, M. L., Lovett, S. T. (2006). RecJ exonuclease: substrates, products and interaction with SSB. Nucleic Acids Res 34: 1084-1091 [Abstract] [Full Text]  
  • Yamagata, A., Kakuta, Y., Masui, R., Fukuyama, K. (2002). The crystal structure of exonuclease RecJ bound to Mn2+ ion suggests how its characteristic motifs are involved in exonuclease activity. Proc. Natl. Acad. Sci. USA 99: 5908-5912 [Abstract] [Full Text]  
  • Yamagata, A., Masui, R., Kakuta, Y., Kuramitsu, S., Fukuyama, K. (2001). Overexpression, purification and characterization of RecJ protein from Thermus thermophilus HB8 and its core domain. Nucleic Acids Res 29: 4617-4624 [Abstract] [Full Text]  
  • Yamagata, A., Kakuta, Y., Masui, R., Fukuyama, K. (2002). The crystal structure of exonuclease RecJ bound to Mn2+ ion suggests how its characteristic motifs are involved in exonuclease activity. Proc. Natl. Acad. Sci. USA 99: 5908-5912 [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»