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    Carbonic anhydrase subunits form a matrix-exposed domain attached to the membrane arm of mitochondrial complex I in plants.

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    Authors
    Sunderhaus, Stephanie
    Dudkina, Natalya V
    Jänsch, Lothar cc
    Klodmann, Jennifer
    Heinemeyer, Jesco
    Perales, Mariano
    Zabaleta, Eduardo
    Boekema, Egbert J
    Braun, Hans-Peter
    Issue Date
    2006-03-10
    
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    Abstract
    Complex I of Arabidopsis includes five structurally related subunits representing gamma-type carbonic anhydrases termed CA1, CA2, CA3, CAL1, and CAL2. The position of these subunits within complex I was investigated. Direct analysis of isolated subcomplexes of complex I by liquid chromatography linked to tandem mass spectrometry allowed the assignment of the CA subunits to the membrane arm of complex I. Carbonate extraction experiments revealed that CA2 is an integral membrane protein that is protected upon protease treatment of isolated mitoplasts, indicating a location on the matrix-exposed side of the complex. A structural characterization by single particle electron microscopy of complex I from the green alga Polytomella and a previous analysis from Arabidopsis indicate a plant-specific spherical extra-domain of about 60 A in diameter, which is attached to the central part of the membrane arm of complex I on its matrix face. This spherical domain is proposed to contain a heterotrimer of three CA subunits, which are anchored with their C termini to the hydrophobic arm of complex I. Functional implications of the complex I-integrated CA subunits are discussed.
    Citation
    Carbonic anhydrase subunits form a matrix-exposed domain attached to the membrane arm of mitochondrial complex I in plants. 2006, 281 (10):6482-8 J. Biol. Chem.
    Affiliation
    Institut für Angewandte Genetik, Universität Hannover, Herrenhäuser Strasse 2, D-30419 Hannover, Germany.
    Journal
    The Journal of biological chemistry
    URI
    http://hdl.handle.net/10033/15332
    DOI
    10.1074/jbc.M511542200
    PubMed ID
    16407270
    Type
    Article
    Language
    en
    ISSN
    0021-9258
    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.M511542200
    Scopus Count
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    publications of the research group cellular proteom research (CPRO)

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