Regulation of Unperturbed DNA Replication by Ubiquitylation

Sara Priego Moreno, Agnieszka Gambus

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)
155 Downloads (Pure)


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.

Original languageEnglish
Pages (from-to)451-468
Number of pages18
Issue number3
Publication statusPublished - 25 Jun 2015


  • DNA replication
  • replisome
  • posttranslational modification
  • termination
  • ubiquitylation
  • proteasomal degradation
  • re-replication


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