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Article: Ubiquitin-dependent regulation of translesion polymerases

TitleUbiquitin-dependent regulation of translesion polymerases
Authors
KeywordsAnaphase-promoting complex (APC)
DNA damage
DNA polymerase
Proliferating cell nuclear antigen (PCNA)
Translesion synthesis
Ubiquitination
Issue Date2010
PublisherPortland Press Ltd. The Journal's web site is located at http://www.biochemsoctrans.org
Citation
Biochemical Society Transactions, 2010, v. 38 n. 1, p. 110-115 How to Cite?
AbstractIn response to DNA damage, TLS (translesion synthesis) allows replicative bypass of various DNA lesions, which stall normal replication. TLS is achieved by low-fidelity polymerases harbouring less stringent active sites. In humans, Y-family polymerases together with Polζ (polymerase ζ) are responsible for TLS across different types of damage. Protein-protein interaction contributes significantly to the regulation of TLS. REV1 plays a central role in TLS because it interacts with all other Y-family members and Polζ. Ubiquitin-dependent regulatory mechanisms also play important roles in TLS. Ubiquitin-binding domains have been found in TLS polymerases and they might be required for TLS activity. Mono-ubiquitination of PCNA (proliferating-cell nuclear antigen), the central scaffold of TLS polymerases, is thought to promote TLS. In addition, both non-proteolytic and proteolytic polyubiquitination of PCNA and TLS polymerases has been demonstrated. Owing to their low fidelity, the recruitment of TLS polymerases is strictly restricted to stalled replication forks. © The Authors Journal compilation.
Persistent Identifierhttp://hdl.handle.net/10722/129102
ISSN
2015 Impact Factor: 2.679
2015 SCImago Journal Rankings: 1.981
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChun, ACSen_HK
dc.contributor.authorJin, DYen_HK
dc.date.accessioned2010-12-23T08:32:31Z-
dc.date.available2010-12-23T08:32:31Z-
dc.date.issued2010en_HK
dc.identifier.citationBiochemical Society Transactions, 2010, v. 38 n. 1, p. 110-115en_HK
dc.identifier.issn0300-5127en_HK
dc.identifier.urihttp://hdl.handle.net/10722/129102-
dc.description.abstractIn response to DNA damage, TLS (translesion synthesis) allows replicative bypass of various DNA lesions, which stall normal replication. TLS is achieved by low-fidelity polymerases harbouring less stringent active sites. In humans, Y-family polymerases together with Polζ (polymerase ζ) are responsible for TLS across different types of damage. Protein-protein interaction contributes significantly to the regulation of TLS. REV1 plays a central role in TLS because it interacts with all other Y-family members and Polζ. Ubiquitin-dependent regulatory mechanisms also play important roles in TLS. Ubiquitin-binding domains have been found in TLS polymerases and they might be required for TLS activity. Mono-ubiquitination of PCNA (proliferating-cell nuclear antigen), the central scaffold of TLS polymerases, is thought to promote TLS. In addition, both non-proteolytic and proteolytic polyubiquitination of PCNA and TLS polymerases has been demonstrated. Owing to their low fidelity, the recruitment of TLS polymerases is strictly restricted to stalled replication forks. © The Authors Journal compilation.en_HK
dc.languageengen_US
dc.publisherPortland Press Ltd. The Journal's web site is located at http://www.biochemsoctrans.orgen_HK
dc.relation.ispartofBiochemical Society Transactionsen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsThe final version of record is available at http://www.biochemsoctrans.org-
dc.subjectAnaphase-promoting complex (APC)en_HK
dc.subjectDNA damageen_HK
dc.subjectDNA polymeraseen_HK
dc.subjectProliferating cell nuclear antigen (PCNA)en_HK
dc.subjectTranslesion synthesisen_HK
dc.subjectUbiquitinationen_HK
dc.subject.meshDNA Damage-
dc.subject.meshDNA Repair-
dc.subject.meshDNA Replication-
dc.subject.meshDNA-Directed DNA Polymerase - genetics - metabolism-
dc.subject.meshUbiquitin - metabolism-
dc.titleUbiquitin-dependent regulation of translesion polymerasesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0300-5127&volume=38 pt. 1&spage=110&epage=115&date=2010&atitle=Ubiquitin-dependent+regulation+of+translesion+polymerases-
dc.identifier.emailJin, DY:dyjin@hkucc.hku.hken_HK
dc.identifier.authorityJin, DY=rp00452en_HK
dc.description.naturepostprint-
dc.identifier.doi10.1042/BST0380110en_HK
dc.identifier.pmid20074045-
dc.identifier.scopuseid_2-s2.0-76449099936en_HK
dc.identifier.hkuros176658en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-76449099936&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume38en_HK
dc.identifier.issue1en_HK
dc.identifier.spage110en_HK
dc.identifier.epage115en_HK
dc.identifier.isiWOS:000274763800020-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridChun, ACS=7003650706en_HK
dc.identifier.scopusauthoridJin, DY=7201973614en_HK

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