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    Studies on interactions of Sarco/Endoplasmic Reticulum Ca2+-ATPase (SERCA) with anti apoptotic protein Bcl-2.

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    umi-ku-2490_1.pdf (1.077Mb)
    Issue Date
    2008-07-29
    Author
    Hewawasam, Geetha S.
    Publisher
    University of Kansas
    Format
    169 pages
    Type
    Dissertation
    Degree Level
    PH.D.
    Discipline
    Chemistry
    Rights
    This item is protected by copyright and unless otherwise specified the copyright of this thesis/dissertation is held by the author.
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    Abstract
    Bcl-2 regulates apoptosis by controlling luminal Ca2+ concentration of endoplasmic reticulum (ER). Dremina et al. reported that Bcl-2 interacts with SERCA, the Ca2+ pump in SR/ER membrane, causing inactivation and translocation. This work reports the characteristics of the SERCA/Bcl-2 interactions using wild type and three mutants, G145E, S24C/C158S and S205C/C158S, of the truncated protein, Bcl-2Δ21. Protein cross-linking, Ca2+-ATPase activity assay, Sucrose Density Gradient fractionation, immunoprecipitation and the fusion protein binding assay are the approaches used. Results reveal that the two proteins can interact with both 1:1 and 2:1 (Bcl-2Δ21: SERCA) molar ratios. The hydrophobic groove of Bcl-2Δ21 is involved in the interactions. The BH1 domain of Bcl-2Δ21 interacts with the ATP binding domain of SERCA. The G145E mutant is a loss-of-function whereas the two Cys-mutants are gain-of-function on SERCA inactivation and translocation. Therefore the conserved residue G145 is a critical hot spot for the Bcl-2Δ21-mediated inactivation and translocation of SERCA.
    URI
    http://hdl.handle.net/1808/4135
    Collections
    • Chemistry Dissertations and Theses [335]
    • Dissertations [4660]

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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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