Ub‐family modifications at the replication fork: Regulating PCNA‐interacting components

@article{Kirchmaier2011UbfamilyMA,
  title={Ub‐family modifications at the replication fork: Regulating PCNA‐interacting components},
  author={A. Kirchmaier},
  journal={FEBS Letters},
  year={2011},
  volume={585}
}
A vast array of proteins is recruited to the replication fork in a dynamic and coordinated manner through physical interactions with Proliferating Cell Nuclear Antigen, PCNA. How this complex exchange of PCNA binding partners is choreographed to ensure proper replication origin licensing, DNA synthesis during normal replication or repair of DNA damage, chromatin assembly, DNA methylation, histone modification, and sister chromatid cohesion is only beginning to be appreciated. In this review… Expand
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References

SHOWING 1-10 OF 157 REFERENCES
SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase
TLDR
It is shown by genetic analysis that SUMO-modified PCNA functionally cooperates with Srs2, a helicase that blocks recombinational repair by disrupting Rad51 nucleoprotein filaments, which suggests a model in whichsumO- modified PCNA recruits SRS2 in S phase in order to prevent unwanted recombination events of replicating chromosomes. Expand
PCNA, the Maestro of the Replication Fork
TLDR
Proliferating cell nuclear antigen -a cofactor of DNA polymerases that encircles DNA-orchestrates several of these functions by recruiting crucial players to the replication fork, indicating that these interactions do not occur simultaneously during replication. Expand
Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p.
TLDR
It is shown that Srs2p physically interacts with sumoylated PCNA, which contributes to the recruitment of the helicase to replication forks, suggesting a mechanism by which SUMO and ubiquitin cooperatively control the choice of pathway for the processing of DNA lesions during replication. Expand
A Role for PCNA Ubiquitination in Immunoglobulin Hypermutation
TLDR
This is the first evidence, to the authors' knowledge, that vertebrates exploit the PCNA-ubiquitin pathway for immunoglobulin hypermutation, most likely through the recruitment of error-prone DNA polymerases. Expand
Replication-Dependent Marking of DNA by PCNA Facilitates CAF-1-Coupled Inheritance of Chromatin
TLDR
It is demonstrated that after DNA replication, replicated, but not unreplicated, DNA is also competent for CAF-1-dependent chromatin assembly and suggested that PCNA and CAf-1 connect DNA replication to chromatinAssembly and the inheritance of epigenetic chromosome states. Expand
PCNA functions as a molecular platform to trigger Cdt1 destruction and prevent re-replication
TLDR
It is reported that replication-dependent proteolysis of Cdt1 requires its interaction with proliferating cell nuclear antigen (PCNA), a homotrimeric processivity factor for DNA polymerases to be inactivated. Expand
PCNA clamp facilitates action of DNA cytosine methyltransferase 1 on hemimethylated DNA
TLDR
This work has shown that DNA cytosine methyltransferase 1 (Dnmt1), which preserves epigenetic signals by completing the methylation of hemimethylated DNA after DNA replication, is one of these PCNA binding proteins that interacts with a number of other proteins to increase their local concentration at replicated DNA sites. Expand
Ubiquitin-Binding Domains in Y-Family Polymerases Regulate Translesion Synthesis
TLDR
The identification of two ubiquitin (Ub)–binding domains (UBM and UBZ), which are evolutionarily conserved in all Y-family TLS polymerases (pols), indicate that Ub-binding domains of Y- family polymerases play crucial regulatory roles in TLS. Expand
A CAF-1–PCNA-Mediated Chromatin Assembly Pathway Triggered by Sensing DNA Damage
TLDR
It is shown that the presence of single-strand breaks and gaps, formed either directly or during DNA damage processing, can trigger the propagation of nucleosomal arrays, which involves the histone chaperone chromatin assembly factor 1 (CAF-1). Expand
Ubiquitin/SUMO modification of PCNA promotes replication fork progression in Xenopus laevis egg extracts
TLDR
It is suggested that PCNA monoubiquitylation serves as a molecular gas pedal that controls the speed of replisome movement during S phase that expands the repertoire of functions for PCNA ubiquitylation and sumoylation by elucidating a role for these modifications during the replication of undamaged DNA. Expand
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