Association of α-subunits with nucleotide-modified β-subunits induces asymmetry in the catalytic sites of the F1-ATPase α3β3-hexamer

Cell Biochemistry and Biophysics

Volumn 39, Issue 3, 2003, Pages 175-181

  Burgard, Sabine ^b   Harada, Mitsuo ^c   Kagawa, Yasuo ^c   Trommer, Wolfgang E ^b   Vogel, Pia D ^a,b  

^a SOUTHERN METHODIST UNIVERSITY   (United States)

^b Rheinland Pfälzische Technische Universität Kaiserslautern Landau   (Germany)

^c JICHI MEDICAL UNIVERSITY   (Japan)

Author keywords

ATP synthase; ESR spectroscopy; Nucleotide binding; Photoaffinity labeling; Spin labels

Indexed keywords

ADENOSINE DIPHOSPHATE; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

ARTICLE; CHEMISTRY; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; PROTEIN CONFORMATION; PROTEIN FOLDING; SPIN LABELING;

ADENOSINE DIPHOSPHATE; BACTERIAL PROTON-TRANSLOCATING ATPASES; CATALYTIC DOMAIN; ELECTRON SPIN RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SUBUNITS; SPIN LABELS;

EID: 2442435773     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/CBB:39:3:175     Document Type: Article

References (35)

1. 1-ATPase from bovine heart mitochondria. Nature 25, 621-628.
2. 1-ATPase complexed with the peptide antibiotic efrapeptin. Proc. Natl. Acad. Sci. USA. 93, 9420-9424.
3. 1-ATPase complexed with the antibiotic inhibitor aurovertin B. Proc. Natl. Acad. Sci. USA. 93, 6913-6917.
4. 1-ATPase: configuration of a critical intermediate in ATP-synthesis/hydrolysis. Proc. Natl. Acad. Sci. USA. 95, 11065-11070.
5. 1-ATPase. Proc. Natl. Acad. Sci USA. 92, 10964-10968.
6. 1-ATPase. Nature 381, 623-625.
7. 1-ATPase. Nature 386, 299-302.
8. 1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer. Structure 15, 825-836.
9. 1-ATP synthase of Escherichia coli. J. Biol. Chem. 39, 3856-3860.
10. Boyer, P.D. (1993) The binding change mechanism for ATP synthase-some probabilities and possibilities. Biochim. Biophys. Acta 1140, 215-250.
11. 1-ATPase as studied by electron spin resonance spectroscopy J. Biol. Chem. 269, 17815.
12. 1-ATPase using electron spin resonance spectroscopy. Spectrochimica Acta, Part A 52, 73-83.
13. 1-ATPase in solution as observed using electron spin resonance spectroscopy. Biochemistry 35, 1188-1193.
14. Vogel P. D. (2000) Insights into the ATP synthase structure and function using affinity and site-specific spin-labeling. J. Bioenergetics Biomembranes 32, 413-421.
15. 1-ATPase. Electron spin resonance spectroscopy and photolabeling by azido-spin-labeled adenine nucleotides support an adenylate kinase-like orientation. J. Biol. Chem. 267, 11982-11986.
16. 1-ATPase. Biochemistry 25, 4431-4437.
17. 1 ATPase: photoaffinity labeling of beta-subunit Tyr-368 at a noncatalytic site and beta Tyr-345 at a catalytic site. Proc. Natl. Acad. Sci. USA. 84, 5715-5719.
18. 1 ATPase. Amino acid sequences of beta-subunit tryptic peptides labeled with 2-azido-ATP. FEBS Lett. 223, 395-401.
19. 1 ATPase. Photoaffinity labeling and peptide sequencing. FEBS Lett. 223, 391-394.
20. 1-ATPase label adjacent tryptic peptides of the beta subunit. Biochem. Biophys. Res. Commun. 154, 854-860.
21. Czarnecki, J. J. (1984) Tautomerism of 2-azidoadenine nucleotides. Effects on enzyme kinetics and photoaffinity labeling. Biochim. Biophys. Acta 800, 41-51.
22. Melese, T. and Boyer, P. D. (1985) Derivatization of the catalytic subunits of the chloroplast ATPase by 2-azido-ATP and dicyclohexylcarbodiimide. Evidence for catalytically induced interchange of the subunits. J. Biol. Chem. 260, 15398-15401.
23. Streckenbach, B., Schwarz, D., and Repke, K. H. R. (1980) Analysis of phosphoryl transfer mechanism and catalytic centre geometries of transport ATPase by means of spin-labelled ATP. Biochim. Biophys. Acta 601, 34-46.
24. 1-ATPase. FEBS Lett. 227, 107-109.
25. Jakobs, P., Sauer, H. E., McIntyre, J. O., Fleischer, S., and Trommer W. E. (1989) Synthesis of spin-labeled 2-azido-ATP: evidence for distinct nucleotide-binding sites in calcium pump protein from sarcoplasmic reticulum. FEBS Lett. 254, 8-12.
26. Ohta, S., Yohda, M., Ishizuka, M., Hirata, H., Hamamoto, T., Otawara-Hamamoto, Y. (1988) Sequence and over-expression of subunits of adenosine triphosphate synthase in thermophilic bacterium PS3. Biochem. Biophys. Acta 933, 141-155.
27. Penefsky, H. S. (1977) Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase J. Biol. Chem. 252, 2891-2899.
28. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
29. Peterson, G. L. (1977) A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 83, 346-356.
30. 1-ATP synthase. FEBS Lett. 178, 10-14.
31. Khananshvili D. and Grometh-Elhanan Z. (1985) Evidence that the Mg-dependent low-affinity binding site for ATP and Pi demonstrated on the isolated beta subunit of the F0.F1 ATP synthase is a catalytic site. Proc. Natl. Acad. Sci. USA. 82, 1886-1890.
32. 1-ATPase. Interaction between nucleotide and aurovertin D binding sites. Biochemistry 23, 6591-6595.
33. 1-subunits requires occupancy of the nucleotide-binding site on beta-subunit by nucleoside triphosphate. J. Biol. Chem. 263, 5569-5573.
34. m70 μm. FEBS Lett. 368, 207-210.
35. Harada, M., Ito, Y., Sato, M., Aono, O., Ohta, S., and Kagawa, Y. (1991) Small-angle X-ray scattering studies of Mg AT(D)P-induced hexamer to dimer dissociation in the reconstituted alpha 3 beta 3 complex of ATP synthase from thermophilic bacterium PS3. J. Biol. Chem. 266, 11455-11460.