F0 Membrane Domain of ATP Synthase from Bovine Heart Mitochondria: Purification, Subunit Composition, and Reconstitution with F1-ATPase

Biochemistry ◽  
1994 ◽  
Vol 33 (25) ◽  
pp. 7971-7978 ◽  
Author(s):  
Ian R. Collinson ◽  
Michael J. Runswick ◽  
Susan K. Buchanan ◽  
Ian M. Fearnley ◽  
J. Mark Skehel ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Subunit Composition ◽  
Heart Mitochondria ◽  
Membrane Domain ◽  
F1 Atpase ◽  
Bovine Heart

ATP Synthase from Bovine Heart Mitochondria In Vitro Assembly of a Stalk Complex in the Presence of F1-ATPase and in its Absence

1994 ◽  
Vol 242 (4) ◽  
pp. 408-421 ◽  
Author(s):  
I COLLINSON ◽  
M VANRAAIJ ◽  
M RUNSWICK ◽  
I FEARNLEY ◽  
J SKEHEL ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Heart Mitochondria ◽  
F1 Atpase ◽  
Bovine Heart ◽  
In Vitro Assembly

scholarly journals ATP Synthase Complex from Bovine Heart Mitochondria

1989 ◽  
Vol 264 (26) ◽  
pp. 15548-15551
Author(s):  
S Joshi ◽  
M J Pringle
Keyword(s):  
Atp Synthase ◽  
Heart Mitochondria ◽  
Bovine Heart

Proton flow through the intramembrane sector of the ATP synthase complex of bovine heart mitochondria

1987 ◽  
Vol 17 (1) ◽  
pp. 147-152
Author(s):  
G. Lippe ◽  
A. Perardi ◽  
M.C. Sorgato ◽  
F. Dabbeni-Sala
Keyword(s):  
Atp Synthase ◽  
Heart Mitochondria ◽  
Bovine Heart ◽  
Flow Through

scholarly journals F1F0-ATP synthase from bovine heart mitochondria: development of the purification of a monodisperse oligomycin-sensitive ATPase

1993 ◽  
Vol 295 (3) ◽  
pp. 799-806 ◽  
Author(s):  
R Lutter ◽  
M Saraste ◽  
H S van Walraven ◽  
M J Runswick ◽  
M Finel ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Atp Hydrolysis ◽  
Gel Filtration ◽  
Primary Objective ◽  
Membrane Domain ◽  
Mitochondrial Membranes ◽  
F1 Atpase ◽  
Ammonium Sulphate Precipitation ◽  
F1f0 Atp Synthase ◽  
Hydrolysis Activity

A new procedure for the isolation of ATP synthase from bovine mitochondria has been developed, with the primary objective of producing enzyme suitable for crystallization trials. Proteins were extracted from mitochondrial membranes with dodecyl-beta-D-maltoside, and the ATP synthase was purified from the extract in the presence of the same detergent by a combination of ion-exchange and gel-filtration chromatography and ammonium sulphate precipitation. This simple and rapid procedure yields 20-30 mg of highly pure and monodisperse enzyme, evidently consisting of 14 different subunits, amongst them, in apparently stoichiometric amounts with the established subunits, subunit e, a recently discovered subunit of unknown function. The enzyme preparation has an oligomycin-sensitive ATP hydrolysis activity, and so the F1 domain is functionally associated with the membrane domain, F0. In contrast with the N-termini of some of the subunits of bovine mitochondrial F1-ATPase, those of the F1F0-ATP synthase are not degraded by proteolysis during the isolation procedure. This preparation therefore satisfies prerequisites for crystallization trials.

PURIFICATION OF F1 - ATPase FROM BOVINE HEART MITOCHONDRIA

1995 ◽  
Vol 23 (4) ◽  
pp. 523S-523S
Author(s):  
GÜLGÜN OKTAY ◽  
HÜSEYIN T. SESSIZ
Keyword(s):  
Heart Mitochondria ◽  
F1 Atpase ◽  
Bovine Heart

scholarly journals The δ-subunit of ATP synthase from bovine heart mitochondria. Complementary DNA sequence of its import precursor cloned with the aid of the polymerase chain reaction

1990 ◽  
Vol 266 (2) ◽  
pp. 421-426 ◽  
Author(s):  
M J Runswick ◽  
S M Medd ◽  
J E Walker
Keyword(s):  
Polymerase Chain Reaction ◽  
Atp Synthase ◽  
Protein Sequence ◽  
Heart Mitochondria ◽  
Cdna Clones ◽  
Mature Protein ◽  
Chain Reaction ◽  
Bovine Heart ◽  
Polymerase Chain ◽  
Delta Subunit

The delta-subunit of ATP synthase from bovine heart mitochondria is part of the extrinsic membrane domain, F1-ATPase. The mature protein is 146 amino acids in length and its function is obscure. It is encoded by a nuclear gene and is imported into the organelle. Two mixtures of oligonucleotides 17 bases long, designed on the basis of the known protein sequence, have been synthesized and employed as primers on bovine cDNA in the polymerase chain reaction. By this means a segment of bovine cDNA encoding part of the delta-subunit has been amplified, and this DNA segment has been employed to identify related cDNA clones in a library. These clones encode the mitochondrial import precursor of the delta-subunit; the protein sequence of the mature protein deduced from it is exactly the same as that determined earlier by direct sequence analysis. The clones have also been used to show that both the bovine and human genomes seem to contain a single gene for the delta-subunit.

scholarly journals The ε-subunit of ATP synthase from bovine heart mitochondria. Complementary DNA sequence, expression in bovine tissues and evidence of homologous sequences in man and rat

1990 ◽  
Vol 265 (2) ◽  
pp. 321-326 ◽  
Author(s):  
O Viñas ◽  
S J Powell ◽  
M J Runswick ◽  
V Iacobazzi ◽  
J E Walker
Keyword(s):  
Dna Sequence ◽  
Atp Synthase ◽  
Protein Sequence ◽  
Nuclear Gene ◽  
Heart Mitochondria ◽  
Amino Acid Residues ◽  
Hybridization Probe ◽  
Related Sequence ◽  
Epsilon Subunit ◽  
Bovine Heart

The epsilon-subunit of ATP synthase from bovine heart mitochondria is assembled into the extrinsic membrane sector, F1-ATPase. The mature protein is 50 amino acid residues in length and its function is unknown. It is a nuclear gene product that is imported into the organelle. A mixture of 64 oligonucleotides 17 bases long, designed on the basis of the known protein sequence, was synthesized and used as a hybridization probe to isolate a cognate cDNA clone from a bovine library. The DNA sequence of this clone was determined, and the protein sequence of the epsilon-subunit deduced from it agrees exactly with that determined by direct sequence analysis of the protein isolated from bovine hearts. The bovine cDNA was used as a hybridization probe to examine the expression of the epsilon-subunit in various bovine tissues. mRNAs related to the cDNA are found in all of these tissues, and no evidence was obtained of the presence of mRNAs for the epsilon-subunit with similar coding sequences and dissimilar 3′ non-coding regions. By hybridization experiments with digests of DNA from cow, man and rat it has been shown that sequences related to the bovine cDNA are present in the genomes of all three species. More than one related sequence was detected in all cases, indicating the presence in all three genomes of more than one gene and/or pseudogenes.

ATP Synthase from Bovine Heart Mitochondria

1994 ◽  
Vol 242 (4) ◽  
pp. 408-421 ◽  
Author(s):  
Ian R. Collinson ◽  
Mark J. van RaaiJ ◽  
Michael J. Runswick ◽  
Ian M. Fearnley ◽  
J.Mark Skehel ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Heart Mitochondria ◽  
Bovine Heart

[11] Structural analysis of ATP synthase from bovine heart mitochondria

1995 ◽  
pp. 163-190 ◽  
Author(s):  
John E. Walker ◽  
Ian R. Collinson ◽  
Mark J. Van Raaij ◽  
Michael J. Runswick
Keyword(s):  
Structural Analysis ◽  
Atp Synthase ◽  
Heart Mitochondria ◽  
Bovine Heart
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