When Hurt Remains

Ben-Shahar, Asaf Rolef; Shalit, Rachel

doi:10.4324/9780429484919

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“…172,173 Both Ctf18-RFC and PCNA bind to the enzyme Eco1, 174,175 which acetylates the Smc3 subunit of cohesin rings as a key step in establishment of sister chromatid cohesion. [176][177][178] The loss of this interaction results in incomplete acetylation of the cohesin complex and slow movement of the replication fork. 179 It is hypothesized that Ctf18-RFC allows the replication fork to transit cohesin rings efficiently, although the mechanism remains mysterious.…”

Section: Alternative Clamp Loadersmentioning

confidence: 99%

Review: The lord of the rings: Structure and mechanism of the sliding clamp loader

Kelch

2016

Biopolymers

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Sliding clamps are ring-shaped polymerase processivity factors that act as master regulators of cellular replication by coordinating multiple functions on DNA to ensure faithful transmission of genetic and epigenetic information. Dedicated AAA+ ATPase machines called clamp loaders actively place clamps on DNA, thereby governing clamp function by controlling when and where clamps are used. Clamp loaders are also important model systems for understanding the basic principles of AAA+ mechanism and function. After nearly 30 years of study, the ATP-dependent mechanism of opening and loading of clamps is now becoming clear. Here I review the structural and mechanistic aspects of the clamp loading process, as well as comment on questions that will be addressed by future studies. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 532-546, 2016.

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Section: Alternative Clamp Loadersmentioning

confidence: 99%

Review: The lord of the rings: Structure and mechanism of the sliding clamp loader

Kelch

2016

Biopolymers

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When Hurt Remains

Cited by 1 publication

References 0 publications

Review: The lord of the rings: Structure and mechanism of the sliding clamp loader

Review: The lord of the rings: Structure and mechanism of the sliding clamp loader

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