The ATP sites of AAA+ clamp loaders work together as a switch to assemble clamps on DNA.

ABSTRACT: Clamp loaders belong to a family of proteins known as ATPases associated with various cellular activities (AAA+). These proteins utilize the energy from ATP binding and hydrolysis to perform cellular functions. The clamp loader is required to load the clamp onto DNA for use by DNA polymerases to increase processivity. ATP binding and hydrolysis are coordinated by several key residues, including a conserved Lys located within the Walker A motif (or P-loop). This residue is required for each subunit to bind ATP. The specific function of each ATP molecule bound to the Saccharomyces cerevisiae clamp loader is unknown. A series of point mutants, each lacking a single Walker A Lys residue, was generated to study the effects of abolishing ATP binding in individual clamp loader subunits. A variety

SUBMITTER: Marzahn MR 

PROVIDER: S-EPMC3937632 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature