Disruption of the bacteriophage T4 Mre11 dimer interface reveals a two-state mechanism for exonuclease activity.

ABSTRACT: The Mre11-Rad50 (MR) complex is a central player in DNA repair and is implicated in the processing of DNA ends caused by double strand breaks. Recent crystal structures of the MR complex suggest that several conformational rearrangements occur during its ATP hydrolysis cycle. A comparison of the Mre11 dimer interface from these structures suggests that the interface is dynamic in nature and may adopt several different arrangements. To probe the functional significance of the Mre11 dimer interface, we have generated and characterized a dimer disruption Mre11 mutant (L101D-Mre11). Although L101D-Mre11 binds to Rad50 and dsDNA with affinity comparable with the wild-type enzyme, it does not activate the ATP hydrolysis activity of Rad50, suggesting that the allosteric communication between Mre1

SUBMITTER: Albrecht DW 

PROVIDER: S-EPMC3438966 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature