TY - JOUR
T1 - DNA-binding and strand-annealing activities of human Mre11
T2 - Implications for its roles in DNA double-strand break repair pathways
AU - De Jager, Martijn
AU - Dronkert, Mies L.G.
AU - Modesti, Mauro
AU - Beerens, Cecile E.M.T.
AU - Kanaar, Roland
AU - Van Gent, Dik C.
PY - 2001/3/15
Y1 - 2001/3/15
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0035869155&partnerID=8YFLogxK
U2 - 10.1093/nar/29.6.1317
DO - 10.1093/nar/29.6.1317
M3 - Article
C2 - 11238998
AN - SCOPUS:0035869155
SN - 0305-1048
VL - 29
SP - 1317
EP - 1325
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - 6
ER -