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  • Structure of the human clamp loader bound to the sliding

    Sep 22, 2020 · Human clamp loader (hRFC) composition and function. ( A ) hRFC consists of five different AAA+ ATPase subunits, named A to E. Each subunit consists of an ATPase module and a …

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  • Replication Clamps and Clamp Loaders

    Aug 01, 2001 · The eukaryotic RFC is a complex consisting of one large and four small subunits. We have determined the crystal structure of the clamp loader small subunit (RFCS) from Pyrococcus furiosus. The six subunits, of which four bind ADP in their canonical nucleotide binding clefts, assemble into a dimer of semicircular trimers.

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  • Division of labor—sequential ATP hydrolysis drives

    Sep 15, 1999 · For a clamp to function as a polymerase tether, it must be assembled at a primed site on DNA where it can bind the polymerase (Stukenberg et al., 1991). This task is performed by a clamp loader, such as the E.coli γ complex, which opens the clamp and facilitates its closure around DNA (Turner et al., 1999).

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  • Human DNA polymerase delta is a pentameric holoenzyme …

    smallest subunit of Polδ is evolutionarily conserved as Cdm1 of Schizosaccharomyces pombe also dimerizes. Thus, we suggest that human Polδ is a pentameric complex with a dimeric p12 subunit, and discuss implications of p12 dimerization in enzyme architecture and …

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  • Crystal Structure of the δ′ Subunit of the Clamp-Loader

    The crystal structure of the δ′ subunit of the clamp-loader complex of E. coli DNA polymerase III has been determined. Three consecutive domains in the structure are arranged in a C-shaped architecture. The N-terminal domain contains a nonfunctional nucleotide binding site. The catalytic component of the clamp-loader complex is the γ subunit, which is homologous to δ′. A sequence

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  • CELLULAR DNA REPLICASES: Components and Dynamics at the

    Jul 07, 2005 · The heteropentameric clamp loaders are circular oligomers, reflecting the circular shape of their respective clamp substrates. Clamps and clamp loaders also function in other DNA metabolic processes, including repair, checkpoint mechanisms, and cell cycle progression. Twin polymerases and clamps coordinate their actions with a clamp loader and

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  • Structure of the human clamp loader reveals an

    Scheme of clamp loader function. (a) The structures of the E. coli β and human PCNA sliding clamps (PDB: 2POL and PDB: AXC, respectively).(b) Schematic of clamp loader function using eukaryotic RFC and PCNA as the example.ATP binding to RFC enables RFC to bind and open PCNA. In the presence of a primed template, RFC places PCNA onto DNA and then hydrolyzes ATP to eject from the PCNA-DNA

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  • Let us know how access to this document benefits you.

    The sliding clamp loader 27. Clamp loader architecture and subunit composition 29 The clamp loader reaction 31 ATP binding 33 Clamp binding 33 Primer/template binding 35 ATP hydrolysis and clamp loader ejection 37 Open questions and Scope of thesis 37 . CHAPTER II: A disease causing variant in PCNA disrupts a promiscuous

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  • A Complex Consisting of Human Replication Factor C p40

    Human replication factor C (hRFC) is a multi-subunit protein complex capable of supporting proliferating cell nuclear antigen (PCNA)-dependent DNA synthesis by DNA polymerases δ and ε. The hRFC complex consists of five different subunits with apparent molecular masses of 140, 40, 38, 37, and 36 kDa. We have previously reported the expression of a three-subunit core complex, consisting of the

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  • American Journal of Physiology-Cell Physiology: Vol 293, No 2

    Aug 01, 2007 · Cover: Double-immunostaining of V-ATPase B1 knockout mouse epididymis showing aquaporin 9 (green) and V-ATPase B2 (red).Nuclei are stained with DAPI (blue). From: Da Silva N, Shum WWC, El-Annan J, Paunescu TG, McKee M, Smith PJS, Brown D, and Breton S. "Relocalization of the V-ATPase B2 subunit to the apical membrane of epididymal clear cells of mice deficient in the B1 subunit."

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  • Motors and switches: AAA+ machines within the replisome

    Clamp loaders from bacteriophage T4, archaea and eukaryotes also contain five subunits, although the composition of the complex varies between different classes of organism.

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  • The RFC Clamp Loader: Structure and Function - Europe PMC

    Scheme of clamp loader function. (a) The structures of the E. coli β and human PCNA sliding clamps (PDB: 2POL and PDB: AXC, respectively).(b) Schematic of clamp loader function using eukaryotic RFC and PCNA as the example.ATP binding to RFC enables RFC to bind and open PCNA. In the presence of a primed template, RFC places PCNA onto DNA and then hydrolyzes ATP to eject from the PCNA-DNA

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  • ( A ) RFC small-subunit apo-protein hexamer viewed from

    Determination of the subunit composition and previous mutational analysis allowed the prediction of the spatial distribution of subunits in this new member of the clamp loader family. Three RFCS1

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  • Clamp Loader ATPases and the Evolution of DNA Replication

    Composition of clamp loaders from the different branches of life. (a) Bacterial clamp loaders consist of three different proteins: δ, δ', and the τ or γ protein (γ, a truncation of the τ protein, is shown here). The δ protein is at the A position, with three copies of the ATPase subunits τ or γ at the B, C and D positions.

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  • American Journal of Physiology-Cell Physiology: Vol 287, No 1

    Jul 01, 2004 · The ubiquitously expressed Na + /H + exchanger isoform 1 (NHE1) functions as a major intracellular pH (pH i) regulatory mechanism in many cell types, and in some tissues its activity may contribute to ischemic injury.In the present study, cortical astrocyte cultures from wild-type (NHE1 +/+) and NHE1-deficient (NHE1 −/−) mice were used to investigate the role of NHE1 in pH i recovery and

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  • Structure of the human clamp loader reveals an

    Feb 18, 2020 · sliding clamp loader (Supplemental Figure 1C-D); the ATPase activity is highest in the presence of both the sliding clamp and Figure 1. Subunit composition and function of the human clamp loader (hRFC). (A) hRFC consists of five different AAA+ ATPase subunits that are named A to E going counterclockwise around the assembly. Each

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  • Replicative DNA Polymerases

    the carboxy-terminal domain of the t subunit of the clamp loader. Because the clamp loader contains two (or three) t subunits, at least two a1u cores are maintained in the replicase com-plex, one each for leading- and lagging-strand synthesis. The 1 subunit has a globular amino-ter-minal exonuclease domain (residues 7–180), E. Johansson and N

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  • ENZYMOLOGY - Jiwaji University

    βsubunit is in the shape of a ring It is termed the clamp protein γsubunit is needed for βto initially clamp onto the DNA It is termed the clamp-loader protein δ, δ' and y subunits are needed for the optimal function of the a and b subunits DNA Polymerase III is a Processive Enzyme 3/27/2020 35

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  • ATP hydrolysis catalyzed by human replication factor C

    Human replication factor C (hRFC) is a five-subunit protein complex (p140, p40, p38, p37, and p36) that acts to catalytically load proliferating cell nuclear antigen onto DNA, where it recruits DNA polymerase δ or to the primer terminus at the expense of ATP, leading to processive DNA synthesis. We have previously shown that a subcomplex of hRFC consisting of three subunits (p40, p37, and p36

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  • How a DNA Polymerase Clamp Loader Opens a Sliding Clamp

    The dimeric ring-shaped sliding clamp of E. coli DNA polymerase III (beta subunit, homolog of eukaryotic PCNA) is loaded onto DNA by the clamp loader gamma complex (homolog of eukaryotic

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