Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (335K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (41)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by de Jager, M.
Right arrow Articles by van Gent, D. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by de Jager, M.
Right arrow Articles by van Gent, D. C.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2001, Vol. 29, No. 6 1317-1325
© 2001 Oxford University Press

DNA-binding and strand-annealing activities of human Mre11: implications for its roles in DNA double-strand break repair pathways

Martijn de Jager1, Mies L. G. Dronkert1, Mauro Modesti1, Cecile E. M. T. Beerens1,2, Roland Kanaar1,2 and Dik C. van Gent1,*

1Department of Cell Biology and Genetics, Erasmus University Rotterdam, Dr Molewaterplein 50, PO Box 1738, 3000 DR Rotterdam, The Netherlands and 2Department of Radiation Oncology, Daniël den Hoed Cancer Center, Rotterdam, The Netherlands

DNA double-strand breaks (DSBs) in eukaryotic cells can be repaired by non-homologous end-joining or homologous recombination. The complex containing the Mre11, Rad50 and Nbs1 proteins has been implicated in both DSB repair pathways, even though they are mechanistically different. To get a better understanding of the properties of the human Mre11 (hMre11) protein, we investigated some of its biochemical activities. We found that hMre11 binds both double- and single-stranded (ss)DNA, with a preference for ssDNA. hMre11 does not require DNA ends for efficient binding. Interestingly, hMre11 mediates the annealing of complementary ssDNA molecules. In contrast to the annealing activity of the homologous recombination protein hRad52, the activity of hMre11 is abrogated by the ssDNA binding protein hRPA. We discuss the possible implications of the results for the role(s) of hMre11 in both DSB repair pathways.

* To whom correspondence should be addressed. Tel: +31 10 408 7932; Fax: +31 10 408 9468; Email: vangent{at}gen.fgg.eur.nl


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
Y. Wu, N. Kantake, T. Sugiyama, and S. C. Kowalczykowski
Rad51 Protein Controls Rad52-mediated DNA Annealing
J. Biol. Chem., May 23, 2008; 283(21): 14883 - 14892.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. W. Nelson and S. J. Benkovic
The T4 Phage UvsW Protein Contains Both DNA Unwinding and Strand Annealing Activities
J. Biol. Chem., January 5, 2007; 282(1): 407 - 416.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
G. Ghosal and K. Muniyappa
Saccharomyces cerevisiae Mre11 is a high-affinity G4 DNA-binding protein and a G-rich DNA-specific endonuclease: implications for replication of telomeric DNA
Nucleic Acids Res., August 22, 2005; 33(15): 4692 - 4703.
[Abstract] [Full Text] [PDF]

Home page
 Mol Cancer ResHome page
H. J. Boeckman, K. S. Trego, and J. J. Turchi
Cisplatin Sensitizes Cancer Cells to Ionizing Radiation via Inhibition of Nonhomologous End Joining
Mol. Cancer Res., May 1, 2005; 3(5): 277 - 285.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Lahdesmaki, A. M. R. Taylor, K. H. Chrzanowska, and Q. Pan-Hammarstrom
Delineation of the Role of the Mre11 Complex in Class Switch Recombination
J. Biol. Chem., April 16, 2004; 279(16): 16479 - 16487.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
J.-L. Ma, E. M. Kim, J. E. Haber, and S. E. Lee
Yeast Mre11 and Rad1 Proteins Define a Ku-Independent Mechanism To Repair Double-Strand Breaks Lacking Overlapping End Sequences
Mol. Cell. Biol., December 1, 2003; 23(23): 8820 - 8828.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
D. Ristic, M. Modesti, R. Kanaar, and C. Wyman
Rad52 and Ku bind to different DNA structures produced early in double-strand break repair
Nucleic Acids Res., September 15, 2003; 31(18): 5229 - 5237.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
J. G. Noordzij, N. S. Verkaik, M. van der Burg, L. R. van Veelen, S. de Bruin-Versteeg, W. Wiegant, J. M. J. J. Vossen, C. M. R. Weemaes, R. de Groot, M. Z. Zdzienicka, et al.
Radiosensitive SCID patients with Artemis gene mutations show a complete B-cell differentiation arrest at the pre-B-cell receptor checkpoint in bone marrow
Blood, February 15, 2003; 101(4): 1446 - 1452.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
M. de Jager, C. Wyman, D. C. van Gent, and R. Kanaar
DNA end-binding specificity of human Rad50/Mre11 is influenced by ATP
Nucleic Acids Res., October 15, 2002; 30(20): 4425 - 4431.
[Abstract] [Full Text] [PDF]

Home page
 Hum Mol GenetHome page
A. Franchitto and P. Pichierri
Protecting genomic integrity during DNA replication: correlation between Werner's and Bloom's syndrome gene products and the MRE11 complex
Hum. Mol. Genet., October 1, 2002; 11(20): 2447 - 2453.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
G. Ira and J. E. Haber
Characterization of RAD51-Independent Break-Induced Replication That Acts Preferentially with Short Homologous Sequences
Mol. Cell. Biol., September 15, 2002; 22(18): 6384 - 6392.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.