About: The Human Cytomegalovirus DNA Polymerase Processivity Factor UL44 Is Modified by SUMO in a DNA-Dependent Manner

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About: The Human Cytomegalovirus DNA Polymerase Processivity Factor UL44 Is Modified by SUMO in a DNA-Dependent Manner Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	The Human Cytomegalovirus DNA Polymerase Processivity Factor UL44 Is Modified by SUMO in a DNA-Dependent Manner
Creator	Palù, Giorgio Winkler, Michael Chiocca, Susanna Urlaub, Henning Alvisi, Gualtiero Loregian, Arianna Mercorelli, Beatrice Hsiao, He-Hsuan Muratore, Giulia Ripalti, Alessandro Sinigalia, Elisa Segré, Chiara
Source	PMC
abstract	During the replication of human cytomegalovirus (HCMV) genome, the viral DNA polymerase subunit UL44 plays a key role, as by binding both DNA and the polymerase catalytic subunit it confers processivity to the holoenzyme. However, several lines of evidence suggest that UL44 might have additional roles during virus life cycle. To shed light on this, we searched for cellular partners of UL44 by yeast two-hybrid screenings. Intriguingly, we discovered the interaction of UL44 with Ubc9, an enzyme involved in the covalent conjugation of SUMO (Small Ubiquitin-related MOdifier) to cellular and viral proteins. We found that UL44 can be extensively sumoylated not only in a cell-free system and in transfected cells, but also in HCMV-infected cells, in which about 50% of the protein resulted to be modified at late times post-infection, when viral genome replication is accomplished. Mass spectrometry studies revealed that UL44 possesses multiple SUMO target sites, located throughout the protein. Remarkably, we observed that binding of UL44 to DNA greatly stimulates its sumoylation both in vitro and in vivo. In addition, we showed that overexpression of SUMO alters the intranuclear distribution of UL44 in HCMV-infected cells, and enhances both virus production and DNA replication, arguing for an important role for sumoylation in HCMV life cycle and UL44 function(s). These data report for the first time the sumoylation of a viral processivity factor and show that there is a functional interplay between the HCMV UL44 protein and the cellular sumoylation system.
has issue date	2012-11-15(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0049630
bibo:pmid	23166733
has license	cc-by
sha1sum (hex)	9fb9a39c7e68fd9c32ab53a6a6ce9af6f1fd2e09
schema:url	https://doi.org/10.1371/journal.pone.0049630
resource representing a document's title	The Human Cytomegalovirus DNA Polymerase Processivity Factor UL44 Is Modified by SUMO in a DNA-Dependent Manner
has PubMed Central identifier	PMC3499415
has PubMed identifier	23166733
schema:publication	PLoS One
resource representing a document's body	covid:9fb9a39c7e68fd9c32ab53a6a6ce9af6f1fd2e09#body_text
is schema:about of	named entity 'sumoylation' named entity 'interaction' named entity 'cell-free system' named entity 'protein' named entity 'extensively' named entity 'PLoS ONE' covid:arg/9fb9a39c7e68fd9c32ab53a6a6ce9af6f1fd2e09 named entity 'system' named entity 'report' named entity 'DNA' named entity 'proteins' named entity 'replication' named entity 'cellular' named entity 'Small' named entity 'holoenzyme' named entity 'During' named entity 'discovered' named entity 'subunit' named entity 'Modified' named entity 'protein' named entity 'life cycle' named entity 'viral genome replication' named entity 'virus' named entity 'HCMV' named entity 'processivity' named entity 'sumoylation' named entity 'SUMO' named entity 'DNA polymerase' named entity 'virus' named entity 'SUMO' named entity 'sumoylation' named entity 'protein' named entity 'HCMV' named entity 'Human Cytomegalovirus' named entity 'SUMO' named entity 'DNA Polymerase' named entity 'SUMO-2' named entity 'lentivirus' named entity 'SUMO-3' named entity 'PFU' named entity 'vector' named entity 'staining' named entity 'DNA polymerization' named entity 'sumoylation' named entity 'processivity' named entity 'Baltimore' named entity 'PCNA' named entity 'protein' named entity 'transduced' named entity 'SUMO' named entity 'SUMO-1' named entity 'protein' named entity 'HCMV' named entity 'bacterial cultures' named entity 'SUMO-3' named entity 'Japan' named entity 'SUMO-1' named entity 'binding to DNA' named entity 'enzyme' named entity 'SUMO-1' named entity 'staining' named entity 'Neo cells' named entity 'Transfected' named entity 'SUMO' named entity 'ubiquitination' named entity 'co-immunoprecipitation' named entity 'PCNA' named entity 'Ubc9' named entity 'SUMO' named entity 'antigen'

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