Zusammenfassung: | |
Complex I of Arabidopsis includes five structurally related subunits representing γ-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 Å 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.
|
|
Lizenzbestimmungen: | CC BY 4.0 Unported - https://creativecommons.org/licenses/by/4.0/ |
Publikationstyp: | Article |
Publikationsstatus: | publishedVersion |
Erstveröffentlichung: | 2006 |
Schlagwörter (englisch): | Biological membranes, Carbonates, Electron microscopy, Liquid chromatography, Mass spectrometry, Proteins, Carbonate extraction experiments, Carbonic anhydrase, Green alga Polytomella, Isolated mitoplasts, Mitochondrial complex I, Plants (botany), calnexin, carbonate dehydratase, membrane protein, mitochondrial complex i enzyme, mitochondrial enzyme, reduced nicotinamide adenine dinucleotide dehydrogenase (ubiquinone), succinate dehydrogenase (ubiquinone), unclassified drug, carbonate dehydratase, mitochondrial protein, peptide hydrolase, protein subunit, reduced nicotinamide adenine dinucleotide dehydrogenase (ubiquinone), Arabidopsis, article, controlled study, electron microscopy, enzyme analysis, enzyme structure, enzyme subunit, green alga, liquid chromatography, mitochondrial membrane, mitochondrion, nonhuman, priority journal, tandem mass spectrometry, Arabidopsis, cell culture, chemistry, enzymology, metabolism, mitochondrion, protein quaternary structure, protein tertiary structure, transmission electron microscopy, ultrastructure, Arabidopsis, Chlorophyta, Polytomella, Algae, Green, Arabidopsis, Carbonic Anhydrases, Cells, Cultured, Electron Transport Complex I, Membrane Proteins, Microscopy, Electron, Transmission, Mitochondria, Mitochondrial Proteins, Peptide Hydrolases, Protein Structure, Quaternary, Protein Structure, Tertiary, Protein Subunits |
Fachliche Zuordnung (DDC): | 570 | Biowissenschaften, Biologie, 540 | Chemie |
Anzeige der Dokumente mit ähnlichem Titel, Autor, Urheber und Thema.