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Structural analysis of a eukaryotic sliding DNA clamp–clamp loader complex
This model, in which the clamp loader complex locks onto primed DNA in a screw-cap-like arrangement, provides a simple explanation for the process by which the engagement of primer–template junctions by the RFC results in ATP hydrolysis and release of the sliding clamp on DNA. Expand
Structure of the C-Terminal Region of p21WAF1/CIP1 Complexed with Human PCNA
The crystal structure of the human DNA polymerase delta processivity factor PCNA (proliferating cell nuclear antigen) complexed with a 22 residue peptide derived from the C-terminus of the cell-cycleExpand
Cellular DNA replicases: components and dynamics at the replication fork.
A heteropentameric AAA+ clamp-loading machine that couples ATP hydrolysis to load circular clamp proteins onto DNA and twin polymerases and clamps coordinate their actions to form a replisome machine that advances the replication fork. Expand
Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp
A potential structural relationship is suggested between the beta subunit and proliferating cell nuclear antigen (PCNA, the eukaryotic polymerase delta [and epsilon] processivity factor), and the gene 45 protein of the bacteriophage T4 DNA polymerase. Expand
Reconstitution of the Mcm2-7p Heterohexamer, Subunit Arrangement, and ATP Site Architecture*
The Mcm2-7p heterohexamer is the presumed replicative helicase in eukaryotic cells and the purified six Saccharomyces cerevisiae MCM proteins as recombinant proteins in Escherichia coli are reconstituted from individual subunits. Expand
Proteomic and genomic characterization of chromatin complexes at a boundary
Specialized assemblies on the Saccharomyces cerevisiae genome that help define and preserve the boundaries that separate silent and active chromatin are dissected, showing that these complexes are important for the faithful maintenance of an established boundary. Expand
The DnaC helicase loader is a dual ATP/ADP switch protein
DnaC is a ‘dual’ switch protein, where both the ATP and the ADP forms are sequentially required for replication, and this dual switching process may underlie the sensitivity of DnaB to even small fluctuations in DnaC levels. Expand
Devoted to the lagging strand—the χ subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly
A role is established for the χ subunit of the γ complex clamp loader in contacting SSB, thus enhancing the clamp loading and processivity of synthesis of the holoenzyme, presumably by helping to localize the Holoenzyme to sites of SSB‐coated ssDNA. Expand
Small-molecule inhibitors of the AAA+ ATPase motor cytoplasmic dynein
The discovery of ciliobrevins is described, the first specific small-molecule antagonists of cytoplasmic dynein, which will be useful reagents for studying cellular processes that require this microtubule motor and may guide the development of additional AAA+ ATPase superfamily inhibitors. Expand
How a DNA Polymerase Clamp Loader Opens a Sliding Clamp
Crystal structures show how the sliding clamp that facilitates processive replication is loaded onto DNA and explain how synergy among the loader, the clamp, and DNA can trigger ATP hydrolysis and release of the closed clamp on DNA. Expand