Molecular analyses of a three-subunit euryarchaeal clamp loader complex from Methanosarcina acetivorans.

ABSTRACT: Chromosomal DNA replication is dependent on processive DNA synthesis. Across the three domains of life and in certain viruses, a toroidal sliding clamp confers processivity to replicative DNA polymerases by encircling the DNA and engaging the polymerase in protein/protein interactions. Sliding clamps are ring-shaped; therefore, they have cognate clamp loaders that open and load them onto DNA. Here we use biochemical and mutational analyses to study the structure/function of the Methanosarcina acetivorans clamp loader or replication factor C (RFC) homolog. M. acetivorans RFC (RFC(Ma)), which represents an intermediate between the common archaeal RFC and the eukaryotic RFC, comprises two different small subunits (RFCS1 and RFCS2) and a large subunit (RFCL). Size exclusion chromatography sugg

SUBMITTER: Chen YH 

PROVIDER: S-EPMC2795300 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature