Cryo-EM structures reveal high-resolution mechanism of a
Sep 23, 2021 · 1 1 Cryo-EM structures reveal high-resolution mechanism of a 2 DNA polymerase sliding clamp loader 3 4 Christl Gaubitza, Xingchen Liua, Joshua Pajaka, Nicholas P. Stonea, Janelle A. Hayesa, Gabriel 5 Demob, Brian A Kelcha¶ 6 7 a Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Chan Medical School, 8 Worcester MA 9 …
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Structure of the human clamp loader bound to the sliding
Structure of the human clamp loader reveals an autoinhibited conformation of a substrate-bound AAA+ switch
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Structure of the human clamp loader bound to the …
Sep 09, 2020 · Significance. DNA replication and repair depend on AAA+ ATPase protein complexes called clamp loaders that open and load ring-shaped sliding clamps onto DNA. Using cryogenic electron microscopy, we determined the first structure of the human clamp loader (RFC), which is in an autoinhibited conformation while bound to the sliding clamp (PCNA).
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Crystal structure of the rad9-rad1-hus1 DNA damage
We have now determined the crystal structure of the human Liming complex, revealing a toroidal structure with a similar architecture to the homotrimeric PCNA DNA-binding clamp. The structure explains the formation of a unique heterotrimeric arrangement and reveals significant differences among the three subunits in the sites implicated in
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Structure of the human clamp loader reveals an
Structure of the human clamp loader reveals an
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How a DNA polymerase clamp loader opens a sliding clamp.
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. One structure reveals that ATP has been hydrolyzed in one subunit, and suggests that clamp closure and ejection of the loader involves disruption of the ATP-dependent match in symmetry.
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Clamp and clamp loader structures of the human checkpoint
In addition, the Rad17-RFC complex was found to be oval in structure and 26 x 22 nm in size with a cleft, reminiscent of the structure of RFC. Conclusion: Our direct comparison of images from the two sets of clamp and clamp loader proteins indicated that RadLiming and Rad17-RFC are, respectively, structural orthologs of PCNA and RFC, with
Get a quoteThe RFC Clamp Loader: Structure and Function
Abstract The eukaryotic RFC clamp loader couples the energy of ATP hydrolysis to open and close the circular PCNA sliding clamp onto primed sites for use by DNA polymerases and repair factors. Structural studies reveal clamp loaders to be heteropentamers. Each subunit contains a region of homology to AAA+ proteins that de Þ nes two domains.
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Structure of the active form of human origin recognition
Jan 23, 2017 · The structure of HsORC reveals a remarkable similarity between two very different ATPases: the replication initiator ORC-CDC6 ATPase and the replication fork DNA polymerase clamp loader (Kelch et al., 2011).Both ATPases function at different times during genome replication but load ring-shaped proteins onto double-stranded DNA so that the ring-shaped …
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Structure of the RAD9-RAD1-HUS1 checkpoint clamp bound to
DNA clamp, a highly conserved ring-shaped protein, binds dsDNA within its central pore. Also, DNA clamp interacts with various nuclear proteins on its front, thereby stimulating their enzymatic activities and biological functions. It has been assumed that the DNA clamp is a functionally single-faced ring from bacteria to humans. Here, we report the crystal structure of the …
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Atomic Structure of the Clamp Loader Small Subunit from
Aug 01, 2001 · In eukaryotic DNA replication, replication factor-C (RFC) acts as the clamp loader, which correctly installs the sliding clamp onto DNA strands at replication forks. 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.
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Mark Hedglin | The Huck Institutes
Structure of the human clamp loader reveals an autoinhibited conformation of a substrate-bound AAA+ switch. Christl Gaubitz, Xingchen Liu, Joseph Magrino, Nicholas P. Stone, Jacob Landeck, Mark Hedglin, Brian A. Kelch, 2020, Proceedings of the National Academy of Sciences of the United States of America on p. 23571-23580
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"Structure of the human clamp loader bound to the sliding
The sliding clamp needs to be actively opened and installed onto DNA by a clamp loader ATPase of the AAA+ family. The human clamp loader Replication Factor C (RFC) and sliding clamp PCNA are both essential and play critical roles in several diseases. Despite decades of study, no structure of human RFC has been resolved.
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The RFC Clamp Loader: Structure and Function
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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"Structure of the human clamp loader bound to the sliding
The sliding clamp needs to be actively opened and installed onto DNA by a clamp loader ATPase of the AAA+ family. The human clamp loader Replication Factor C (RFC) and sliding clamp PCNA are both essential and play critical roles in several diseases. Despite decades of study, no structure of human RFC has been resolved.
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Dual Roles of Ctf18-RFC: Loading the Clamp and - Structure
Jan 02, 2018 · Clamp loaders such as Ctf18-RFC assist DNA replication by loading the PCNA clamp onto DNA. In this issue of Structure, Grabarczyk et al. (2018) reveal that a hook-like structure formed by the unique Dcc1 and Ctf8 subunits mediates the interaction of Ctf18-RFC with the leading strand DNA polymerase ɛ.
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ORCID
Structure of the human clamp loader reveals an autoinhibited conformation of a substrate-bound AAA+ switch. Proceedings of the National Academy of Sciences Liming | journal-article DOI: 10.1073/pnas.2007437117 Show more detail. Source: Crossref Structure of the human clamp loader bound to the sliding clamp: a further twist on AAA+ mechanism
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Structure of the human clamp loader reveals an
Structure of the human clamp loader reveals an
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"Structure of the human clamp loader bound to the sliding
Feb 18, 2020 · SUMMARY. DNA replication requires the sliding clamp, a ring-shaped protein complex that encircles DNA, where it acts as an essential cofactor for DNA polymerases and other proteins. The sliding clamp needs to be actively opened and installed onto DNA by a clamp loader ATPase of the AAA+ family. The human clamp loader Replication Factor C (RFC) and …
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Motors and switches: AAA+ machines within the replisome
Nov 01, 2002 · Structure of the human clamp loader reveals an autoinhibited conformation of a substrate-bound AAA+ switch. Gaubitz C, Liu X, Magrino J, Stone NP, Landeck J, Hedglin M, Kelch BA. Proc Natl Acad Sci U S A, 117(38):23571-23580, 09 Sep 2020 Cited by: 3 articles | PMID: 32907938 | PMCID: PMC7519235
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