Clamp Loader Complex - University of California Berkeley

Clamp Loader Complex - University of California Berkeley

Crystal structure of the chi:psi subassembly of the

Jan 07, 2004 · The chi (χ) and psi (ψ) subunits of Escherichia coli DNA polymerase III form a heterodimer that is associated with the ATP-dependent clamp-loader machinery. In E. coli, the χ:ψ heterodimer serves as a bridge between the clamp-loader complex and the single-stranded DNA-binding protein.We determined the crystal structure of the χ:ψ heterodimer at 2.1 Å resolution.

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Allosteric communication in DNA polymerase clamp loaders

Apr 13, 2021 · Department of Molecular and Cell Biology, University of California, Berkeley, United States; California Institute for Quantitative Biosciences (QB3), University of California, Berkeley, We purified the wild-type clamp-loader complex, the Q118N mutant complex, and the Q118N/I141L double mutant that has partial recovery of fitness in the

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Structural analysis of the inactive state of the

How a DNA Polymerase Clamp Loader Opens a Sliding Clamp

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(PDF) Open clamp structure in the clamp-loading complex

Molecular Analyses of a Three-Subunit Euryarchaeal Clamp Loader Complex from Methanosarcina acetivorans. By Roderick Mackie. Reverse-Chaperoning Activity of an AAA+ Protein. By Isaac K.o Cann and T. Earnest. Computational analysis of DNA replicases in double-stranded DNA viruses: relationship with the genome size

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Out-of-plane motions in open sliding clamps: molecular

How a DNA Polymerase Clamp Loader Opens a Sliding Clamp

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Mapping the interaction of DNA with the Escherichia coli

Author information: (1)Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA. Sliding clamps are loaded onto DNA by ATP-dependent clamp loader complexes.

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Nucleotide-Induced Conformational Changes in an Isolated

University of California, Berkeley tide-freestate [9].The -ATPase, wrench,and stator Berkeley, California 94720 subunits are related to each other structurally, and to 3 Physical Biosciences Division the subunits of eukaryotic and archaeal clamp loader Lawrence Berkeley National Laboratory complexes known as replication factor C (RFC) [9, 15–

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Eric R. Goedken - Publications

Analysis of the role of PCNA-DNA contacts during clamp loading. Bmc Structural Biology. 10: 3. PMID 20113510 DOI: 10.1186/1472-Kefid : 1: 2009: Simonetta KR, Kazmirski SL, Goedken ER, Cantor AJ, Kelch BA, McNally R, Seyedin SN, Makino DL, O'Donnell M, Kuriyan J. The mechanism of ATP-dependent primer-template recognition by a clamp loader

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RESEARCH ARTICLE Open Access Analysis of the role of …

To bind, open, and load the clamp on DNA, the clamp loader executes a cycle of ATP binding and hydrolysis. ATP binding allows for the formation of a stable complex between the clamp loader and an open clamp [18,19]. Upon binding primer-template DNA [20], ATP hydrolysis is stimulated, and results in the release of the clamp on DNA (Figure 1B

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Research News: - Berkeley Lab — Lawrence Berkeley

Jul 17, 2006 · For the E.coli study, Berger and his team utilized the exceptionally bright and intense x-rays of Beamline 8.3.1 at Berkeley Lab's Advanced Light Source synchrotron. With the data gathered at this protein crystallography facility, Berger and his team assembled a high-resolution model of the molecular structure of a protein known as DnaA, which is a member of …

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How a DNA polymerase clamp loader opens a sliding clamp

Dec 01, 2011 · Thus, recognition of the DNA target by a clamp:clamp loader complex triggers the disassembly of the loader complex and the release of the closed clamp on DNA. As shown previously for the E. coli clamp loader complex bound to DNA( 15 ), the AAA+ modules of the ATP-loaded clamp loader are organized symmetrically, so that they match the geometry

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Lec 4 DNA replication .pdf - Bacterial DNA replication is

University of California, Berkeley • MCELLBI 102. KEY_MCB 102 Midterm 2 Practice Exam_Wildermuth.pdf Each core has a 2-protein sliding clamp enclosing the DNA The clamp loader proteins tether together the two cores Clamp loader can lock together exactly once — initiating twice at some origins would cause persistent replication

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John Kuriyan - University of California, Berkeley

We are currently applying high-throughput mutagenesis methods to these systems to understand the functioning of the AAA+ ATPases that form the core of the clamp-loader complexes. Biography. Dr. Kuriyan is also Chancellor's Professor at the University of California, Berkeley.

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How a DNA Polymerase Clamp Loader Opens a Sliding Clamp

Dec 23, 2011 · We present structures for the ATP-bound state of the clamp loader complex from bacteriophage T4, bound to an open clamp and primer-template DNA. The clamp loader traps a spiral conformation of the open clamp so that both the loader and the clamp match the helical symmetry of DNA. University of California, Berkeley, CA 94720, USA. 2 Howard

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Structural analysis of the inactive state of the

Nov 19, 2004 · Clamp-loader complexes are heteropentameric AAA+ ATPases that load sliding clamps onto DNA. The structure of the nucleotide-free Escherichia coli clamp loader had been determined previously and led to the proposal that the clamp-loader cycles between an inactive state, in which the ATPase domains form a closed ring, and an active state that opens up to …

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Allosteric communication in DNA polymerase clamp loaders

Apr 13, 2021 · Department of Molecular and Cell Biology, University of California, Berkeley, United States; California Institute for Quantitative Biosciences (QB3), University of California, The structure of the complete clamp-loader complex is shown, with the surfaces of the four central-coupler units depicted. (PDB ID: 3u60 Kelch et al., 2011).

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Lec 4 DNA replication .pdf - Bacterial DNA replication is

University of California, Berkeley • MCELLBI 102. KEY_MCB 102 Midterm 2 Practice Exam_Wildermuth.pdf Each core has a 2-protein sliding clamp enclosing the DNA The clamp loader proteins tether together the two cores Clamp loader can lock together exactly once — initiating twice at some origins would cause persistent replication

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RCSB PDB - 1XXH: ATPgS Bound E. Coli Clamp Loader Complex

Nov 05, 2004 · Clamp-loader complexes are heteropentameric AAA+ ATPases that load sliding clamps onto DNA. The structure of the nucleotide-free Escherichia coli clamp loader had been determined previously and led to the proposal that the clamp-loader cycles between an inactive state, in which the ATPase domains form a closed ring, and an active state that opens up to …

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The Mechanism of ATP-Dependent Primer-Template Recognition

Clamp loaders load sliding clamps onto primer-template DNA. The structure of the E. coli clamp loader bound to DNA reveals the formation of an ATP-dependent spiral of ATPase domains that tracks only the template strand, allowing recognition of both RNA and DNA primers. Unlike hexameric helicases, in which DNA translocation requires distinct conformations of the …

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Structural analysis of the inactive state of the

Nov 30, 2004 · (1)Department of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA. Clamp-loader complexes are heteropentameric AAA+ ATPases that load sliding clamps onto DNA.

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