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

2.50
Hdl Handle:
http://hdl.handle.net/10033/15332
Title:
Carbonic anhydrase subunits form a matrix-exposed domain attached to the membrane arm of mitochondrial complex I in plants.
Authors:
Sunderhaus, Stephanie; Dudkina, Natalya V; Jänsch, Lothar ( 0000-0002-5655-1181 ) ; Klodmann, Jennifer; Heinemeyer, Jesco; Perales, Mariano; Zabaleta, Eduardo; Boekema, Egbert J; Braun, Hans-Peter
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.
Affiliation:
Institut für Angewandte Genetik, Universität Hannover, Herrenhäuser Strasse 2, D-30419 Hannover, Germany.
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.
Journal:
The Journal of biological chemistry
Issue Date:
10-Mar-2006
URI:
http://hdl.handle.net/10033/15332
DOI:
10.1074/jbc.M511542200
PubMed ID:
16407270
Type:
Article
Language:
en
ISSN:
0021-9258
Appears in Collections:
Publications of RG Cellular Proteome Research (CPRO)

Full metadata record

DC FieldValue Language
dc.contributor.authorSunderhaus, Stephanieen
dc.contributor.authorDudkina, Natalya Ven
dc.contributor.authorJänsch, Lotharen
dc.contributor.authorKlodmann, Jenniferen
dc.contributor.authorHeinemeyer, Jescoen
dc.contributor.authorPerales, Marianoen
dc.contributor.authorZabaleta, Eduardoen
dc.contributor.authorBoekema, Egbert Jen
dc.contributor.authorBraun, Hans-Peteren
dc.date.accessioned2007-12-17T09:45:15Zen
dc.date.available2007-12-17T09:45:15Zen
dc.date.issued2006-03-10en
dc.identifier.citationCarbonic 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.en
dc.identifier.issn0021-9258en
dc.identifier.pmid16407270en
dc.identifier.doi10.1074/jbc.M511542200en
dc.identifier.urihttp://hdl.handle.net/10033/15332en
dc.description.abstractComplex 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.en
dc.language.isoenen
dc.subject.meshAlgae, Greenen
dc.subject.meshArabidopsisen
dc.subject.meshCarbonic Anhydrasesen
dc.subject.meshCells, Cultureden
dc.subject.meshElectron Transport Complex Ien
dc.subject.meshMembrane Proteinsen
dc.subject.meshMicroscopy, Electron, Transmissionen
dc.subject.meshMitochondriaen
dc.subject.meshMitochondrial Proteinsen
dc.subject.meshPeptide Hydrolasesen
dc.subject.meshProtein Structure, Quaternaryen
dc.subject.meshProtein Structure, Tertiaryen
dc.subject.meshProtein Subunitsen
dc.titleCarbonic anhydrase subunits form a matrix-exposed domain attached to the membrane arm of mitochondrial complex I in plants.en
dc.typeArticleen
dc.contributor.departmentInstitut für Angewandte Genetik, Universität Hannover, Herrenhäuser Strasse 2, D-30419 Hannover, Germany.en
dc.identifier.journalThe Journal of biological chemistryen

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