• Admin Login
    View Item 
    •   Home
    • Research Institute in Healthcare Science
    • Research Institute in Healthcare Science
    • View Item
    •   Home
    • Research Institute in Healthcare Science
    • Research Institute in Healthcare Science
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of WIRECommunitiesTitleAuthorsIssue DateSubmit DateSubjectsTypesJournalDepartmentPublisherThis CollectionTitleAuthorsIssue DateSubmit DateSubjectsTypesJournalDepartmentPublisher

    Administrators

    Admin Login

    Local Links

    AboutThe University LibraryOpen Access Publications PolicyDeposit LicenceCOREWIRE Copyright and Reuse Information

    Statistics

    Display statistics

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

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Authors
    Owen, Rhiannon M.
    Baker, Rachael D.
    Bader, Scott
    Dunlop, Malcolm G.
    Nicholl, Iain D.
    Issue Date
    2007
    
    Metadata
    Show full item record
    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
    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
    Journal article
    Language
    en
    ISSN
    1021-335X
    Collections
    Research Institute in Healthcare Science

    entitlement

    Related articles

    • Mismatch repair in methylated DNA. Structure and activity of the mismatch-specific thymine glycosylase domain of methyl-CpG-binding protein MBD4.
    • Authors: Wu P, Qiu C, Sohail A, Zhang X, Bhagwat AS, Cheng X
    • Issue date: 2003 Feb 14
    • 5-Methylcytosine DNA glycosylase activity is also present in the human MBD4 (G/T mismatch glycosylase) and in a related avian sequence.
    • Authors: Zhu B, Zheng Y, Angliker H, Schwarz S, Thiry S, Siegmann M, Jost JP
    • Issue date: 2000 Nov 1
    • Crystal structure of human methyl-binding domain IV glycosylase bound to abasic DNA.
    • Authors: Manvilla BA, Maiti A, Begley MC, Toth EA, Drohat AC
    • Issue date: 2012 Jul 13
    • Excision of thymine and 5-hydroxymethyluracil by the MBD4 DNA glycosylase domain: structural basis and implications for active DNA demethylation.
    • Authors: Hashimoto H, Zhang X, Cheng X
    • Issue date: 2012 Sep 1
    • Crystal structure of the mismatch-specific thymine glycosylase domain of human methyl-CpG-binding protein MBD4.
    • Authors: Zhang W, Liu Z, Crombet L, Amaya MF, Liu Y, Zhang X, Kuang W, Ma P, Niu L, Qi C
    • Issue date: 2011 Sep 2
    DSpace software (copyright © 2002 - 2023)  DuraSpace
    Quick Guide | Contact Us
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.