A covalent tandem dimer of the mitochondrial ADP/ATP carrier is functional in vivo
| Autor: | C. Fiore, Agnès Le Saux, Claudine David, Véronique Trézéguet, Guy J.-M. Lauquin, A.C. Dianoux, Céline Gourdet, Gérard Brandolin |
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| Jazyk: | angličtina |
| Předmět: |
Models
Molecular Topography Saccharomyces cerevisiae Proteins Stereochemistry Dimer Covalent tandem dimer Molecular Sequence Data Biophysics Saccharomyces cerevisiae Biochemistry Fungal Proteins chemistry.chemical_compound Adenine nucleotide Subunit stoichiometry Nucleotide Amino Acid Sequence Cloning Molecular Inner mitochondrial membrane Integral membrane protein chemistry.chemical_classification Chemistry Nuclear Proteins Cell Biology Intracellular Membranes Transmembrane protein Mitochondria Covalent bond ADP/ATP carrier ATP–ADP translocase Dimerization Mitochondrial ADP ATP Translocases Plasmids |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Bioenergetics. (1-2):81-93 |
| ISSN: | 0005-2728 |
| DOI: | 10.1016/S0005-2728(99)00115-2 |
| Popis: | The adenine nucleotide carrier, or Ancp, is an integral protein of the inner mitochondrial membrane. It is established that the inactive Ancp bound to one of its inhibitors (CATR or BA) is a dimer, but different contradictory models were proposed over the past years to describe the organization of the active Ancp. In order to decide in favor of a single model, it is necessary to establish the orientations of the N- and C-termini and thus the parity of the Ancp transmembrane segments (TMS). According to this, we have constructed a gene encoding a covalent tandem dimer of the Saccharomyces cerevisiae Anc2p and we demonstrate that it is stable and active in vivo as well as in vitro. The properties of the isolated dimer are strongly similar to those of the native Anc2p, as seen from nucleotide exchange and inhibitor binding experiments. We can therefore conclude that the native Anc2p has an even number of TMS and that the N- and C-terminal regions are exposed to the same cellular compartment. Furthermore, our results support the idea of a minimal dimeric functional organization of the Ancp in the mitochondrial membrane and we can suggest that TMS 1 of one monomer and TMS 6 of the other monomer in the native dimer are very close to each other. |
| Databáze: | OpenAIRE |
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