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Formation of the yeast F1F0-ATP synthase dimeric complex does not require the ATPase inhibitor protein, Inh1. J Biol Chem 2002 Oct 18;277(42):39289-95

Date

08/09/2002

Pubmed ID

12167646

DOI

10.1074/jbc.M205720200

Abstract

The yeast F1F0-ATP synthase forms dimeric complexes in the mitochondrial inner membrane and in a manner that is supported by the F0-sector subunits, Su e and Su g. Furthermore, it has recently been demonstrated that the binding of the F1F0-ATPase natural inhibitor protein to purified bovine F1-sectors can promote their dimerization in solution (Cabezon, E., Arechaga, I., Jonathan P., Butler, G., and Walker J. E. (2000) J. Biol. Chem. 275, 28353-28355). It was unclear until now whether the binding of the inhibitor protein to the F1 domains contributes to the process of F1F0-ATP synthase dimerization in intact mitochondria. Here we have directly addressed the involvement of the yeast inhibitor protein, Inh1, and its known accessory proteins, Stf1 and Stf2, in the formation of the yeast F1F0-ATP synthase dimer. Using mitochondria isolated from null mutants deficient in Inh1, Stf1, and Stf2, we demonstrate that formation of the F(1)F(0)-ATP synthase dimers is not adversely affected by the absence of these proteins. Furthermore, we demonstrate that the F1F0-ATPase monomers present in su e null mutant mitochondria can be as effectively inhibited by Inh1, as its dimeric counterpart in wild-type mitochondria. We conclude that dimerization of the F1F0-ATP synthase complexes involves a physical interaction of the membrane-embedded F0 sectors from two monomeric complexes and in a manner that is independent of inhibitory activity of the Inh1 and accessory proteins.

Author List

Dienhart M, Pfeiffer K, Schagger H, Stuart RA

Author

Rosemary Stuart PhD Professor in the Biology department at Marquette University




MESH terms used to index this publication - Major topics in bold

Adaptor Proteins, Signal Transducing
Adenosine Triphosphatases
Adenosine Triphosphate
Dimerization
Electrophoresis, Polyacrylamide Gel
Fungal Proteins
Hydrogen-Ion Concentration
Hydrolysis
Mitochondria
Mitochondrial Proteins
Protein Binding
Proton-Translocating ATPases
Saccharomyces cerevisiae Proteins
Time Factors
jenkins-FCD Prod-482 91ad8a360b6da540234915ea01ff80e38bfdb40a