Regulation of the mitochondrial ATP synthase/ATPase complex: cDNA cloning, sequence, overexpression, and secondary structural characterization of a functional protein inhibitor

Archives of Biochemistry and Biophysics
M S Lebowitz, P L Pedersen

Abstract

The ATPase inhibitor protein of the rat liver mitochondrial ATP synthase/ATPase complex has been cloned from a rat liver cDNA library, and its nucleotide sequence determined. The sequence is highly homologous to both the bovine heart (approximately 70%) and the yeast inhibitor proteins (approximately 40%). The deduced protein sequence is 107 amino acids in length, and based on homology to the bovine heart protein, the first 25 N-terminal amino acids encode a putative mitochondrial targeting sequence. The "mature" protein (without the targeting sequence) fused to the maltose binding protein has been overexpressed in Escherichia coli. The maltose binding protein was used as a handle for the development of a rapid one-step purification of the fusion protein by affinity chromatography on an amylose resin. The purified fusion protein was cleaved with Factor Xa protease at the fusion junction, and the resulting ATPase inhibitor protein was purified to > 90% purity. The purified, overexpressed inhibitor protein displays normal inhibitor activity. The protein inhibits ATP hydrolysis catalyzed by the ATP synthase/ATPase complex in submitochondrial particles in a manner kinetically indistinguishable from the same protein purified from ra...Continue Reading

Citations

Dec 5, 2008·Microbiology and Molecular Biology Reviews : MMBR·Sangjin Hong, Peter L Pedersen
Feb 9, 2000·Bioscience, Biotechnology, and Biochemistry·N IchikawaY Masazumi
Oct 31, 2001·FEBS Letters·L Domínguez-RamírezM Tuena de Gómez-Puyou
Jun 6, 2000·Biochimica Et Biophysica Acta·D W Green, G J Grover
Jun 1, 1995·Biochimica Et Biophysica Acta·D S SamuelS H Chan
Dec 1, 1994·Current Opinion in Structural Biology·J E Walker
Oct 18, 2006·Biochemistry·José J GarcíaJosé S Rodríguez-Zavala

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