regulation of unperturbed dna replication by ubiquitylation

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ID: 181161
2015
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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.
Reference Key
moreno2015genesregulation Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Sara Priego Moreno;Agnieszka Gambus
Journal thermal science and engineering progress
Year 2015
DOI
10.3390/genes6030451
URL
http://www.mdpi.com/2073-4425/6/3/451
Keywords
ubiquitylation dna replication termination

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