γε sub-complex of thermophilic ATP synthase has the ability to bind ATP

Biochemical and Biophysical Research Communications

Volumn 349, Issue 4, 2006, Pages 1368-1371

  Iizuka, Satoshi ^a   Kato, Shigeyuki ^a   Yoshida, Masasuke ^b   Kato Yamada, Yasuyuki ^a  

^a RIKKYO UNIVERSITY   (Japan)

^b TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

subunit; ATP binding; ATP synthase; F1; FoF1

Indexed keywords

ADENOSINE TRIPHOSPHATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PROTEIN SUBUNIT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME REGULATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN SYNTHESIS; THERMOPHILIC BACTERIUM; BACILLUS; BINDING SITE; CHEMISTRY; ENZYME ACTIVATION; ENZYMOLOGY; PROTEIN TERTIARY STRUCTURE;

ADENOSINE TRIPHOSPHATE; BACILLUS; BINDING SITES; ENZYME ACTIVATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; PROTON-TRANSLOCATING ATPASES;

EID: 33748758703     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.09.001     Document Type: Article

References (28)

1. Boyer P.D. The ATP synthase-a splendid molecular machine. Annu. Rev. Biochem. 66 (1997) 717-749
2. Yoshida M., Muneyuki E., and Hisabori T. ATP synthase-a marvellous rotary engine of the cell. Nat. Rev. Mol. Cell Biol. 2 (2001) 669-677
3. 1-ATPase from bovine heart mitochondria. Nature 370 (1994) 621-628
4. 1-ATPase. J. Biol. Chem. 273 (1998) 19375-19377
5. Smith J.B., Sternweis P.C., and Heppel L.A. Partial purification of active delta and epsilon subunits of the membrane ATPase from Escherichia coli. J. Supramol. Struct. 3 (1975) 248-255
6. 1 ATPase. Arch. Biochem. Biophys. 197 (1979) 83-89
7. Sternweis P.C., and Smith J.B. Characterization of the inhibitory (epsilon) subunit of the proton-translocating adenosine triphosphatase from Escherichia coli. Biochemistry 19 (1980) 526-531
8. Wilkens S., Dahlquist F.W., McIntosh L.P., Donaldson L.W., and Capaldi R.A. Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy. Nat. Struct. Biol. 2 (1995) 961-967
9. Uhlin U., Cox G.B., and Guss J.M. Crystal structure of the epsilon subunit of the proton-translocating ATP synthase from Escherichia coli. Structure 5 (1997) 1219-1230
10. o-type ATPase. J. Biol. Chem. 271 (1996) 13888-13891
11. 1 ATPase by disulfide bond formation. Effect on nucleotide binding affinities of the catalytic sites. J. Biol. Chem. 271 (1996) 32623-32628
12. 1-ATPase is activated without dissociation of an endogenous inhibitor, epsilon subunit. J. Biol. Chem. 272 (1997) 24906-24912
13. o complex of Escherichia coli cross-linking studies show the same structure in situ as when isolated. J. Biol. Chem. 274 (1999) 28351-28355
14. 1-ATPase. J. Biol. Chem. 274 (1999) 33991-33994
15. 1-ATPase. J. Biol. Chem. 275 (2000) 35746-35750
16. Rodgers A.J.W., and Wilce M.C.J. Structure of the gamma-epsilon complex of ATP synthase. Nat. Struct. Biol. 7 (2000) 1051-1054
17. 1-ATPase at 2.4 Å resolution. Nat. Struct. Biol. 7 (2000) 1055-1061
18. 1-ATPase: propagation of the inhibitory effect of the epsilon subunit. J. Biol. Chem. 276 (2001) 23969-23973
19. o ATP synthase provide a ratchet action to regulate this rotary motor enzyme. Proc. Natl. Acad. Sci. USA 98 (2001) 6560-6564
20. 1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of epsilon subunit in response to proton motive force and ADP/ATP balance. J. Biol. Chem. 278 (2003) 46840-46846
21. 1-ATPase binds ATP. J. Biol. Chem. 278 (2003) 36013-36016
22. 1-ATPase. J. Biol. Chem. 280 (2005) 40130-40134
23. 1-ATPase binds ATP. FEBS Lett. 579 (2005) 6875-6878
24. Stock D., Leslie A.G., and Walker J.E. Molecular architecture of the rotary motor in ATP synthase. Science 286 (1999) 1700-1705
25. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
26. 1. Eur. J. Biochem. 247 (1997) 1158-1165
27. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
28. 1 ATPase binds the epsilon subunit. J. Biol. Chem. 257 (1982) 7354-7359