结构生物学sturcture biology explore-28.pdfVIP

217 Clamp loaders and sliding clamps David Jeruzalmi*??, Mike O’Donnell? and John Kuriyan*?§ A coherent view of the structure and function of DNA transcription in T4 bacteriophage [22], DNA repair and polymerase processivity factors (sliding clamps and clamp cell cycle control [23]. loaders) is emerging from recent structural studies. Crystal structures of sliding clamps from the T4 and RB69 Sliding clamps are loaded onto DNA by specialized protein bacteriophages, and from an archaebacterium expand the complexes known as clamp loaders [24–26]. Clamp loaders gallery of ring-shaped processivity factors and clarify how the are ATP-fueled molecular machines that open the sliding clamp interacts with the DNA polymerase. Crystallographic clamp and load them onto primed DNA [27,28,29?,30]. and electron microscopic views of clamp loaders from Clamp loaders are conserved across evolution [31,32] and bacteria, archaebacteria and eukaryotes emphasize their their subunits are members of the AAA+ family of common architecture and have produced models of how ATPases [33]. The bacterial clamp loader is composed ATP binding might be coupled to clamp opening/loading. of five subunits in a stoichiometry of γ3δδ′ [24,34?,35]. Additionally, two subunits (χ and ψ) are associated with Addresses the clamp loader and couple it to single stranded DNA *Departments of Molecular and Cell Biology, and of Chemistry, binding protein [36–38], but are not essential for clamp Howard Hughes Medical Institute, The University of California, loading [39]. The γ subunits harbor functional ATP-binding Berkeley, CA 94720, USA ? sites and are the motors that couple ATP binding to cla