The identification of a novel alternatively spliced form of the MBD4 DNA glycosylase.

2.50
Hdl Handle:
http://hdl.handle.net/2436/29448
Title:
The identification of a novel alternatively spliced form of the MBD4 DNA glycosylase.
Authors:
Owen, Rhiannon M.; Baker, Rachael D.; Bader, Scott; Dunlop, Malcolm G.; Nicholl, Iain D.
Abstract:
Methyl-CpG binding protein 4 (MBD4) is a mismatch-specific G:T and G:U DNA glycosylase. During an analysis of MBD4 expression in HeLa cells we noted the presence of an unexpectedly short reverse transcribed product. This cDNA lacked the region encoding the methyl-binding domain and exon 3 of MBD4 but retained the glycosylase domain. Sequence comparison indicates the existence of a previously unreported cryptic splice site in the MBD4 genomic sequence thus illuminating a mechanism whereby a glycosylase acquired a methyl-binding capacity, thus targeting potential mutagenic CpG sites. In vitro assays of this highly purified species, refolded in arginine rich conditions, confirmed that this unique, short version of MBD4 possessed uracil DNA glycosylase but not thymine DNA glycosylase activity. We conclude that the identification of a transcript encoding a short version of MBD4 indicates that MBD4 expression may be more complex than previously reported, and is worthy of further investigation.
Citation:
Oncology Reports, 17(1): 111-116
Publisher:
Spandidos Publications Ltd
Journal:
Oncology Reports
Issue Date:
2007
URI:
http://hdl.handle.net/2436/29448
PubMed ID:
17143486
Additional Links:
http://www.spandidos-publications.com/or/article.jsp?article_id=or_17_1_111
Type:
Article
Language:
en
ISSN:
1021-335X
Appears in Collections:
Cancer Research Group

Full metadata record

DC FieldValue Language
dc.contributor.authorOwen, Rhiannon M.-
dc.contributor.authorBaker, Rachael D.-
dc.contributor.authorBader, Scott-
dc.contributor.authorDunlop, Malcolm G.-
dc.contributor.authorNicholl, Iain D.-
dc.date.accessioned2008-06-04T10:37:57Z-
dc.date.available2008-06-04T10:37:57Z-
dc.date.issued2007-
dc.identifier.citationOncology Reports, 17(1): 111-116en
dc.identifier.issn1021-335X-
dc.identifier.pmid17143486-
dc.identifier.urihttp://hdl.handle.net/2436/29448-
dc.description.abstractMethyl-CpG binding protein 4 (MBD4) is a mismatch-specific G:T and G:U DNA glycosylase. During an analysis of MBD4 expression in HeLa cells we noted the presence of an unexpectedly short reverse transcribed product. This cDNA lacked the region encoding the methyl-binding domain and exon 3 of MBD4 but retained the glycosylase domain. Sequence comparison indicates the existence of a previously unreported cryptic splice site in the MBD4 genomic sequence thus illuminating a mechanism whereby a glycosylase acquired a methyl-binding capacity, thus targeting potential mutagenic CpG sites. In vitro assays of this highly purified species, refolded in arginine rich conditions, confirmed that this unique, short version of MBD4 possessed uracil DNA glycosylase but not thymine DNA glycosylase activity. We conclude that the identification of a transcript encoding a short version of MBD4 indicates that MBD4 expression may be more complex than previously reported, and is worthy of further investigation.en
dc.language.isoenen
dc.publisherSpandidos Publications Ltden
dc.relation.urlhttp://www.spandidos-publications.com/or/article.jsp?article_id=or_17_1_111en
dc.subjectMBD4en
dc.subjectDNA repairen
dc.subject.meshAlternative Splicingen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshBase Sequenceen
dc.subject.meshCodonen
dc.subject.meshEndodeoxyribonucleasesen
dc.subject.meshHela Cellsen
dc.subject.meshHumansen
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshProtein Isoformsen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshRNA, Messengeren
dc.subject.meshReverse Transcriptase Polymerase Chain Reactionen
dc.titleThe identification of a novel alternatively spliced form of the MBD4 DNA glycosylase.en
dc.typeArticleen
dc.identifier.journalOncology Reportsen

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