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Poster

The characterization and analysis of Pap10 in mitochondria

Alwaleed Alkhaja1, Markus Deckers, Peter Rehling
1 Georg August Universität Göttingen, Biochemie II, Göttingen, Germany

Abstract

The F1FO ATP synthase plays a major role in oxidative phosphorylation by utilizing the proton gradient across the mitochondrial inner membrane to generate ATP from ADP and inorganic phosphate. The F1FO ATP synthase, which spans the mitochondrial inner membrane, can be found as monomeric species or associated into homo-dimers. Moreover, higher oligomers of the F1FO ATP synthase formed by homo-dimers have been found in various organisms. The higher oligomeric states of the enzyme are involved in mitochondrial ultrastructure by promoting membrane curvature and cristae membrane formation. By using a sequence motif screen to identify novel dimerization factors of the F1FO ATP synthase, we have identified a previously uncharacterized mitochondrial protein, which we termed Pap10. Here we analyzed ATPase association and function of Pap10 in mitochondria.


DOI®: 10.3288/contoo.paper.1562
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