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    The amino-terminal TPR domain of Dia2 tethers SCF(Dia2) to the replisome progression complex.

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    Authors
    Morohashi, Hiroko
    Maculins, Timurs
    Labib, Karim
    Affiliation
    Cancer Research UK Paterson Institute for Cancer Research, University of Manchester, UK.
    Issue Date
    2009-12-01
    
    Metadata
    Show full item record
    Abstract
    Eukaryotic cells contain multiple versions of the E3 ubiquitin ligase known as the SCF (Skp1/cullin/F box), each of which is distinguished by a different F box protein that uses a domain at the carboxyl terminus to recognize substrates [1, 2]. The F box protein Dia2 is an important determinant of genome stability in budding yeast [3-5], but its mode of action is poorly understood. Here we show that SCF(Dia2) associates with the replisome progression complex (RPC) that assembles around the MCM2-7 helicase at DNA replication forks [6]. This interaction requires the RPC components Mrc1 and Ctf4, both of which associate with a tetratricopeptide repeat (TPR) domain located at the amino terminus of Dia2. Our data indicate that the TPR domain of Dia2 tethers SCF(Dia2) to the RPC, probably increasing the local concentration of the ligase at DNA replication forks. This regulation becomes important in cells that accumulate stalled DNA replication forks at protein-DNA barriers, perhaps aiding the interaction of SCF(Dia2) with key substrates. Our findings suggest that the amino-terminal domains of other F box proteins might also play an analogous regulatory role, controlling the localization of the cognate SCF complexes.
    Citation
    The amino-terminal TPR domain of Dia2 tethers SCF(Dia2) to the replisome progression complex. 2009, 19 (22):1943-9 Curr. Biol.
    Journal
    Current Biology
    URI
    http://hdl.handle.net/10541/109303
    DOI
    10.1016/j.cub.2009.09.062
    PubMed ID
    19913425
    Type
    Article
    Language
    en
    ISSN
    1879-0445
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.cub.2009.09.062
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research
    Medical Oncology

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