A role for the yeast PCNA unloader Elg1 in eliciting the
Jul 22, 2019 · Eukaryotic clamp loaders and unloaders in the maintenance of genome stability. Lee KY, Park SH. Exp Mol Med, 52(12):1948-1958, 18 Dec 2020 Cited by: 0 articles | PMID: 33339954 | PMCID: PMC8080817. Review Free to read & use
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New Insights into Replication Clamp Unloading - ScienceDirect
Nov 29, 2013 · The sliding clamp PCNA acts as an essential interaction platform during DNA replication. • Elg1/ATAD shares homology with clamp loaders and promotes genomic stability. • Posttranslational modifications of PCNA impinge upon yeast and human Elg1/ATAD5. • Two reports have now implicated Elg1/ATAD5 in PCNA unloading during replication.
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The replisome guides nucleosome assembly during DNA
Mar 12, 2020 · The RFC complex functions as a sliding clamp loader and unloader, which is conserved from yeast to human cells . There are three isoforms of RFCs participating in DNA replication, Rfc1-RFC, Ctf18-RFC and the Elg1-RFC complex, which differ in their largest subunits [ 113 ].
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Clamp loader ATPases and the evolution of DNA replication
Apr 20, 2012 · In the case of bacterial clamp loaders, it is clear that only the B, C, and D subunits are active ATPases. The eukaryotic clamp loaders contain five subunits that can bind ATP, but activity appears to be necessary only in the B, C, and D subunits. The E site can bind nucleotide, but lacks catalytic activity.
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Clamp loading, unloading and intrinsic stability of the
clamp loaders in each of these systems are composed of multiple subunits. The E. coli clamp loader is the five-subunit complex, the eukaryotic clamp loader is the five protein RF-C (also called activator-1) and the T4 clamp loader is the gene protein 44/62 complex (also a five subunit structure, reviewed in Kelman & O'Donnell 1994).
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Eukaryotic clamp loaders and unloaders in the …
Dec 18, 2020 · Europe PMC is an archive of life sciences journal literature.
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Allosteric communication in DNA polymerase clamp loaders
Apr 13, 2021 · Sliding DNA clamps and the ATP-driven clamp-loader complexes that load them onto DNA are essential components of the DNA replication machinery in all branches of life (Yao and O'Donnell, 2016).Sliding clamps, such as proliferating cell nuclear antigen (PCNA) in eukaryotes, are ring-shaped proteins that enable highly processive DNA replication by tethering DNA polymerases to the template
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10.1016/S1367-5931(97)80068-3 | DeepDyve
Jun 11, 2020 · Recently, the eukaryotic clamp-loader from both humans and yeast (RF-C) has been reconstituted from its five purified subunits [ZS,Z9]. While the exact functions of the individual clamp-loader subunits remain largely unknown, the overall role of the clamp-loader is to chaperone the clamp to the primer/template and catalyze ring opening.
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Clamp loader ATPases and the evolution of DNA replication
Apr 20, 2012 · Clamp loaders are pentameric ATPases of the AAA+ family that operate to ensure processive DNA replication. They do so by loading onto DNA the ring-shaped sliding clamps that tether the polymerase to the DNA. Structural and biochemical analysis of clamp loaders has shown how, despite differences in composition across different branches of life, all clamp loaders undergo the …
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Eukaryotic clamp loaders and unloaders in the …
Dec 18, 2020 · PCNA unloading. After completion of DNA synthesis during DNA replication and repair, PCNA is unloaded from DNA by the eukaryotic clamp unloader ATAD5-RLC (Elg1-RLC in yeast) 10,16,17,30.The RFC complex can unload PCNA in vitro 9, even though its activity is significantly lower than that of ATAD5-RLC 10.It has been reported that yeast Ctf18-RLC can unload PCNA in vitro when …
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DNA clamp - Wikipedia
A DNA clamp, also known as a sliding clamp or β-clamp, is a protein complex that serves as a processivity-promoting factor in DNA replication.As a critical component of the DNA polymerase III holoenzyme, the clamp protein binds DNA polymerase and prevents this enzyme from dissociating from the template DNA strand. The clamp-polymerase protein–protein interactions are stronger and more
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The Kinetics of Gamma Complex, the Escherichia Coli Clamp
In addition, binding of the bacterial and eukaryotic clamp loaders to p/t DNA triggers rapid ATP hydrolysis and dissociation of the clamp loader from the DNA, such that the clamp loader DNA complex is transient and not likely to be long lived enough to efficiently bind clamps (75,97) Nonproductive interactions between the clamp loaders and DNA
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Mechanism of Processivity Clamp Opening by the Delta
The dimeric ring-shaped sliding clamp of E. coli DNA polymerase III (β subunit, homolog of eukaryotic PCNA) is loaded onto DNA by the clamp loader γ complex (homolog of eukaryotic Replication Factor C, RFC). The δ subunit of the γ complex binds to the β ring and opens it. The crystal structure of a β:δ complex shows that δ, which is structurally related to the δ′ and γ subunits of
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New Insights into Replication Clamp Unloading - ScienceDirect
Nov 29, 2013 · The sliding clamp PCNA acts as an essential interaction platform during DNA replication. • Elg1/ATAD shares homology with clamp loaders and promotes genomic stability. • Posttranslational modifications of PCNA impinge upon yeast and human Elg1/ATAD5. • Two reports have now implicated Elg1/ATAD5 in PCNA unloading during replication.
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Eukaryotic clamp loaders and unloaders in the …
PCNA appears as a functional hub on replicating and replicated chromosomal DNA and has an essential role in the maintenance genome integrity in proliferating cells.Eukaryotes have multiple paralogues of sliding clamp, PCNA and its loader, RFC.
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Clamp loader ATPases and the evolution of DNA replication
Apr 20, 2012 · In the case of bacterial clamp loaders, it is clear that only the B, C, and D subunits are active ATPases. The eukaryotic clamp loaders contain five subunits that can bind ATP, but activity appears to be necessary only in the B, C, and D subunits. The E site can bind nucleotide, but lacks catalytic activity.
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Functions of Multiple Clamp and Clamp-Loader Complexes in
Jan 23, 2018 · This alternative clamp-loader system transmits DNA-damage signals in genomic DNA to the checkpoint-activation network and the DNA-repair apparatus. Another two alternative loader complexes, CTF18-RFC and ELG1-RFC, have roles that are distinguishable from the …
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How a DNA Polymerase Clamp Loader Opens a Sliding Clamp
Sliding clamps cannot load onto DNA spontaneously because they are closed circles (5, 10, 11) ().Instead, adenosine triphosphate (ATP)–dependent complexes known as clamp loaders open the sliding clamps and load them onto primed DNA in the correct orientation for productive engagement of the polymerase [the clamp loaders are the γ/τ complex in bacteria, replication factor–C (RFC) in
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