Journal
GENES
Volume 6, Issue 3, Pages 451-468Publisher
MDPI AG
DOI: 10.3390/genes6030451
Keywords
DNA replication; ubiquitylation; proteasomal degradation; re-replication; termination; posttranslational modification; replisome
Categories
Funding
- U.K. Medical Research Council Career
- Birmingham Fellows Fellowship
- [MR/K007106/1]
- MRC [MR/K007106/1] Funding Source: UKRI
- Medical Research Council [MR/K007106/1] Funding Source: researchfish
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Posttranslational modification of proteins by means of attachment of a small globular protein ubiquitin (i.e., ubiquitylation) represents one of the most abundant and versatile mechanisms of protein regulation employed by eukaryotic cells. Ubiquitylation influences almost every cellular process and its key role in coordination of the DNA damage response is well established. In this review we focus, however, on the ways ubiquitylation controls the process of unperturbed DNA replication. We summarise the accumulated knowledge showing the leading role of ubiquitin driven protein degradation in setting up conditions favourable for replication origin licensing and S-phase entry. Importantly, we also present the emerging major role of ubiquitylation in coordination of the active DNA replication process: preventing re-replication, regulating the progression of DNA replication forks, chromatin re-establishment and disassembly of the replisome at the termination of replication forks.
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