Glutamic acid in the inhibitory site of mitochondrial ATPase inhibitor, IF1, participates in pH sensing in both mammals and yeast

Journal of Biochemistry

Volumn 144, Issue 4, 2008, Pages 547-553

  Ando, Chiyoko ^a   Ichikawa, Naoki ^a  

^a Osaka Prefecture University   (Japan)

Author keywords

ATP synthase (F1Fo ATPase); IF1 (ATPase inhibitor); Mitochondria; pH sensing; Regulation

Indexed keywords

AMINO ACID; FUNGAL PROTEIN; GLUTAMIC ACID; HISTONE; MUTANT PROTEIN; PROTEIN IF1; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE INHIBITOR; TETRAMER; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; COW; ENZYME INHIBITION; GENE MUTATION; GENE OVEREXPRESSION; NONHUMAN; PH MEASUREMENT; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN FOLDING; PROTEIN PURIFICATION; SENSITIZATION; YEAST;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BASE SEQUENCE; CATTLE; DNA PRIMERS; GLUTAMIC ACID; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEINS; PROTON-TRANSLOCATING ATPASES; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY;

BOVINAE; MAMMALIA;

EID: 53549109128     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvn100     Document Type: Article

References (23)

1. 1-ATPase from bovine heart mitochondria. Nature 370, 621-628
2. Boyer, P.D. (1997) The ATP synthase - a splendid molecular machine. Annu. Rev. Biochem. 66, 717-749
3. Pullman, M.E. and Monroy, G.C. (1963) A naturally occurring inhibitor of mitochondrial adenosine triphosphatase. J. Biol. Chem. 238, 3762-3769
4. Klein, G., Satre, M., and Vignais, P. (1977) Natural protein ATPase inhibitor from Candida utilis mitochondria. Binding properties of the radiolabeled inhibitor. FEBS Lett. 84, 129-134
5. Sah, J.F., Kumar, C., and Mohanty, P. (1993) pH dependent conformational changes modulate functional activity of the mitochondrial ATPase inhibitor protein. Biochem. Biophys. Res. Commun. 194, 1521-1528
6. Ichikawa, N. and Ogura, C. (2003) Overexpression, purification, and characterization of human and bovine mitochondrial ATPase inhibitors: comparison of the properties of mammalian and yeast ATPase inhibitors. J. Bioenerg. Biomembr. 35, 399-407
7. 1-ATPase. Biochim. Biophys. Acta 1292, 241-248
8. 1, by pH. J. Biol. Chem. 275, 25460-25464
9. Ichikawa, N., Karaki, A., Kawabata, M., Ushida, S., Mizushima, M., and Hashimoto, T. (2001) The region from phenylalanine-17 to phenylalanine-28 of a yeast mitochondrial ATPase inhibitor is essential for its ATPase inhibitory activity. J. Biochem. 130, 687-693
10. Ichikawa, N., Fukuda, M., Hashimoto, T., and Tagawa, K. (1998) The carboxyl-terminal region of the yeast ATPase inhibitor is indispensable for the stability of the protein in mitochondria. J. Biochem. 124, 886-891
11. Ichikawa, N., Yoshida, Y., Hashimoto, T., Ogasawara, N., Yoshikawa, H., Imamoto, F., and Tagawa, K. (1990) Activation of ATP hydrolysis by an uncoupler in mutant mitochondria lacking an intrinsic ATPase inhibitor in yeast. J. Biol. Chem. 265, 6274-6278
12. 2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem. 257, 13028-13033
13. Ichikawa, N., Nakabayashi, K., and Hashimoto, T. (2002) A yeast mitochondrial ATPase inhibitor interacts with three proteins that are easy to dissociate from the mitochondrial inner membrane. J. Biochem. 132, 649-654
14. Walker, J.E., Gay, N.J., Powell, S.J., Kostina, M., and Dyer, M.R. (1987) ATP synthase from bovine mitochondria: sequences of imported precursors of oligomycin sensitivity conferral protein, factor 6, and adenosinetriphosphatase inhibitor protein. Biochemistry 26, 8613-8619
15. Higuchi, R. (1989) Using PCR to engineer DNA in PCR Technology (Erlich, H. A. ed) pp. 61-70, Stockton Press, New York
16. Kitamura, M., Kojima, S., Ogasawara, K., Nakaya, T., Sagara, T., Niki, K., Miura, K., Akutsu, H., and Kumagai, I. (1994) Novel FMN-binding protein from Desulfovibrio vulgaris (Miyazaki F). Cloning and expression of its gene in Escherichia coli. J. Biol. Chem. 269, 5566-5573
17. Lowry, O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275
18. Allen, R.J.L. (1940) The estimation of phosphorus. Biochem. J. 34, 858-865
19. Horstman, L.L. and Racker, E. (1970) Partial resolution of the enzymes catalyzing oxidative phosphorylation. XXII. Interaction between mitochondrial adenosine triphosphatase inhibitor and mitochondrial adenosine triphosphatase. J. Biol. Chem. 245, 1336-1344
20. Davies, G.E. and Stark, G.R. (1970) Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins. Proc. Natl Acad. Sci. USA 66, 651-656
21. 1-ATPase but cannot be transported to yeast mitochondria. J. Bioenerg. Biomembr. 38, 93-99
22. 1-ATPase from bovine mitochondria. Proc. Natl Acad. Sci. USA 104, 15671-15676
23. van Raaij, M.J., Orriss, G.L., Montgomery, M.G., Runswick, M.J., Fearnley, I.M., Skehel, J.M., and Walker, J.E. (1996) The ATPase inhibitor protein from bovine heart mitochondria: the minimal inhibitory sequence. Biochemistry 35, 15618-15625