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Review
. 2012;13(2):1858-1885.
doi: 10.3390/ijms13021858. Epub 2012 Feb 10.

Yeast mitochondrial interactosome model: metabolon membrane proteins complex involved in the channeling of ADP/ATP

Benjamin Clémençon  1
Affiliations
Review

Yeast mitochondrial interactosome model: metabolon membrane proteins complex involved in the channeling of ADP/ATP

Benjamin Clémençon. Int J Mol Sci. 2012.

Abstract

The existence of a mitochondrial interactosome (MI) has been currently well established in mammalian cells but the exact composition of this super-complex is not precisely known, and its organization seems to be different from that in yeast. One major difference is the absence of mitochondrial creatine kinase (MtCK) in yeast, unlike that described in the organization model of MI, especially in cardiac, skeletal muscle and brain cells. The aim of this review is to provide a detailed description of different partner proteins involved in the synergistic ADP/ATP transport across the mitochondrial membranes in the yeast Saccharomyces cerevisiae and to propose a new mitochondrial interactosome model. The ADP/ATP (Aacp) and inorganic phosphate (PiC) carriers as well as the VDAC (or mitochondrial porin) catalyze the import and export of ADP, ATP and Pi across the mitochondrial membranes. Aacp and PiC, which appear to be associated with the ATP synthase, consist of two nanomotors (F(0), F(1)) under specific conditions and form ATP synthasome. Identification and characterization of such a complex were described for the first time by Pedersen and co-workers in 2003.

Keywords: ADP/ATP carrier; ATP synthasome; VDAC; diffusion; inorganic phosphate carrier; metabolic microcompartmentation; metabolon; mitochondrial interactosome; phosphotransfer network.

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Figures

Figure 1
Figure 1
Conformational states adopted by the ADP/ATP carrier during the nucleotides transport. carboxyatractyloside (CATR) and bongkrekic acid (BA) inhibit the transition by locking the carrier in stable complexes.
Figure 2
Figure 2
Primary sequence alignment of bovine ADP/ATP carrier (Ant1p) and ADP/ATP carrier (Aac2p). Sequence alignment was performed with the Needle program. The bars show the identical amino acids and the two points the similar residue. Numbering refers to the Aac2p sequence. Both sequences are 49.5% identical.
Figure 3
Figure 3
Structure of mitochondrial porins (a) Isoform 1 of human porin obtained by NMR spectroscopy [120] (1) and by an approach combining both NMR spectroscopy and X-ray crystallography [119] (2); (b) High-resolution structure of an isoform of the murine Voltage-Dependent Anion Channel (VDAC1) solved by X-ray crystallography [121]. All these structures exhibit a channel formed by 19 stranded antiparallel β-sheets in the transmembrane core protein. The N-and C-terminal ends are oriented towards the cytosol. These structures classify protein VDAC in a new family of porins. The N-terminus is an organized structure (α-helix) or not, whose orientation differs from one model to another.
Figure 4
Figure 4
Machinery model of active transport driven by the electrochemical gradient of protons across the mitochondrial membranes. (a) The inorganic phosphate (Pi) and ADP3− are imported into the matrix via two carriers: Aac2p and PiC while the matrix ATP4− is consumed by the ATP synthase, shown in its monomeric form. The charge of each transported molecule is indicated. The membrane potential is negative in the matrix. The outer membrane ensures free passage of these compounds though the VDAC, noted Por1p; (b) Gel electrophoresis showing the co-purification of Aac2p, PiC and Por1p from a yeast mitochondria lysate in n-dodecyl-β-D-maltoside/emulphogen mix (DDM/EM) after chromatography on a hydroxylapatite column (Coomassie Blue staining of the SDS-PAGE gel).
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References

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