Abstract：
:MRE11 and RAD50 are known to be required for nonhomologous joining of DNA ends in vivo. We have investigated the enzymatic activities of the purified proteins and found that Mre11 by itself has 3' to 5' exonuclease activity that is increased when Mre11 is in a complex with Rad50. Mre11 also exhibits endonuclease activity, as shown by the asymmetric opening of DNA hairpin loops. In conjunction with a DNA ligase, Mre11 promotes the joining of noncomplementary ends in vitro by utilizing short homologies near the ends of the DNA fragments. Sequence identities of 1-5 base pairs are present at all of these junctions, and their diversity is consistent with the products of nonhomologous end-joining observed in vivo.
journal_name
Mol Celljournal_title
Molecular cellauthors
Paull TT,Gellert Mdoi
10.1016/s1097-2765(00)80097-0subject
Has Abstractpub_date
1998-06-01 00:00:00pages
969-79issue
7eissn
1097-2765issn
1097-4164pii
S1097-2765(00)80097-0journal_volume
1pub_type
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