Regulation of Unperturbed DNA Replication by Ubiquitylation

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Colleges, School and Institutes

Abstract

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.

Details

Original languageEnglish
Pages (from-to)451-468
Number of pages18
JournalGenes
Volume6
Issue number3
Publication statusPublished - 25 Jun 2015

Keywords

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