Evidence for three α subunits in one molecule of F1-ATPase from thermophilic bacterium PS3

1978 ◽  
Vol 84 (1) ◽  
pp. 117-122 ◽  
Author(s):  
Masasuke Yoshida ◽  
Nobuhito Sone ◽  
Hajime Hirata ◽  
Yasuo Kagawa
Keyword(s):  
Thermophilic Bacterium ◽  
F1 Atpase ◽  
Α Subunits

scholarly journals Photoaffmity cross-linking of F1 ATPase from the thermophilic bacterium PS 3 by 3'-arylazido-β-alanyl-8-azido ATP

FEBS Letters ◽  
1985 ◽  
Vol 186 (2) ◽  
pp. 275-280 ◽  
Author(s):  
Hans-Jochen Schäfer ◽  
Gabriele Rathgeber ◽  
Klaus Dose ◽  
Y. Masafumi ◽  
Y. Kagawa
Keyword(s):  
Thermophilic Bacterium ◽  
Cross Linking ◽  
F1 Atpase

F1 ATPase from the thermophilic bacterium PS3 (TF1) shows ATP modulation of oxygen exchange

Biochemistry ◽  
1989 ◽  
Vol 28 (17) ◽  
pp. 6949-6954 ◽  
Author(s):  
Vladimir N. Kasho ◽  
Masasuke Yoshida ◽  
Paul D. Boyer
Keyword(s):  
Thermophilic Bacterium ◽  
Oxygen Exchange ◽  
F1 Atpase

Three-Dimensional Structure of F1-ATPase of Thermophilic Bacterium PS3 Obtained by Electron Crystallography

1993 ◽  
Vol 113 (2) ◽  
pp. 245-250 ◽  
Author(s):  
Noriyuki Ishii ◽  
Hideyuki Yoshimura ◽  
Kuniaki Nagayama ◽  
Yasuo Kagawa ◽  
Masasuke Yoshida
Keyword(s):  
Three Dimensional ◽  
Thermophilic Bacterium ◽  
Dimensional Structure ◽  
Electron Crystallography ◽  
Three Dimensional Structure ◽  
F1 Atpase

Structure–function relationships of A-, F- and V-ATPases

2001 ◽  
Vol 204 (15) ◽  
pp. 2597-2605 ◽  
Author(s):  
Gerhard Grüber ◽  
Helmut Wieczorek ◽  
William R. Harvey ◽  
Volker Müller
Keyword(s):  
Structure Function ◽  
Recent Work ◽  
Atp Hydrolysis ◽  
Three Dimensional ◽  
Electrochemical Potential ◽  
F1 Atpase ◽  
Cellular Energy ◽  
Structural Relationships ◽  
Physical Linkage ◽  
Α Subunits

SUMMARY Ion-translocating ATPases, such as the F1Fo-, V1Vo- and archaeal A1Ao enzymes, are essential cellular energy converters which transduce the chemical energy of ATP hydrolysis into transmembrane ionic electrochemical potential differences. Based on subunit composition and primary structures of the subunits, these types of ATPases are related through evolution; however, they differ with respect to function. Recent work has focused on the three-dimensional structural relationships of the major, nucleotide-binding subunits A and B of the A1/V1-ATPases and the corresponding β and α subunits of the F1-ATPase, and the location of the coupling subunits within the stalk that provide the physical linkage between the regions of ATP hydrolysis and ion transduction. This review focuses on the structural homologies and diversities of A1-, F1- and V1-ATPases, in particular on significant differences between the stalk regions of these families of enzymes.

scholarly journals Isolation of α-subunits of factor F1 from submitochondrial particles and the reconstitution of active ATPase from isolated α-subunits and β-subunits bound to the mitochondrial membrane

1980 ◽  
Vol 192 (2) ◽  
pp. 483-488 ◽  
Author(s):  
I A Kozlov ◽  
Y M Milgrom ◽  
I S Tsybovski
Keyword(s):  
Atpase Activity ◽  
Active Site ◽  
Mitochondrial Membrane ◽  
Iodoacetic Acid ◽  
Reduced Form ◽  
Beta Subunits ◽  
Submitochondrial Particles ◽  
F1 Atpase ◽  
Alpha Subunits ◽  
Α Subunits

The alpha-subunits of factor-F1 ATPase are removed by extraction of submitochondrial particles with 1.75 M-LiCl, with the consequent loss of ATPase activity. ATPase activity is reconstituted by incubation of LiCl-extracted particles with purified alpha-subunits, and the reconstituted ATPase activity is oligomycin-sensitive. Reconstitution is enhanced by maintenance of the alpha-subunits in reduced form by dithiothreitol or NaBH4 and by modification of the alpha-subunits by p-chloromercuribenzoate, iodoacetic acid or N-ethylmaleimide. Experiments with the mixed anhydride of ATP and mesitylene-carboxylic acid, which was previously shown to interact with the F1 active site, localized on the beta-subunits, indicate that the active site of ATPase is shielded by the alpha-subunits.

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