2chv

Publication Abstract from PubMed

We have investigated the communication between subunits in replication factor C (RFC) from Archaeoglobus fulgidus. Mutation of the proposed arginine finger in the small subunits results in a complex that can still bind ATP but has impaired clamp-loading activity, a process that normally only requires binding of nucleotide. The small subunit alone forms a hexameric ring that is six-fold symmetric in the absence of ATP. However, this symmetry is broken when the nucleotide is bound to the complex. A conformational change associated with nucleotide binding may relate to the opening of PCNA rings by RFC during the loading reaction. The structures also reveal the importance of the N-terminal helix of each subunit at the ATP-binding site. Analysis of mutant protein complexes containing subunits lacking this N-terminal helix reveals key distinct regulatory roles during clamp loading that are different for the large and small subunits in the RFC complex.

Communication between subunits within an archaeal clamp-loader complex.,Seybert A, Singleton MR, Cook N, Hall DR, Wigley DB EMBO J. 2006 May 17;25(10):2209-18. Epub 2006 Apr 20. PMID:16628222^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.