Mutations at histidine 211 of the yeast F1-ATPase β-subunit affect the stability and assembly of the ATPase and the structure of the active site

Archives of Biochemistry and Biophysics

Volumn 326, Issue 1, 1996, Pages 126-136

  Schnizer, Richard A ^a   Schuster, Sheldon M ^a  

^a UNIVERSITY OF FLORIDA   (United States)

Author keywords

assembly; F1 ATPase; intragenic suppressor; Saccharomyces cerevisiae

Indexed keywords

ADENOSINE TRIPHOSPHATASE;

ARTICLE; MUTATION; PRIORITY JOURNAL; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE; YEAST;

SACCHAROMYCES CEREVISIAE;

EID: 0030059062     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1006/abbi.1996.0056     Document Type: Article

References (50)

1. Kagawa, Y. (1984) in Bioenergetics (Ernster, L., Ed.), pp. 149-186, Elsevier Science, B.V. Amsterdam.
2. Senior, A. (1988) Physiol. Rev. 68, 177-231.
3. Penefsky, H., and Cross, R. (1991) in Advances in Enzymology and Related Areas of Molecular Biology (Meister, A., Ed.), Vol. 64, pp. 173-214, Wiley, New York.
4. Hatefi, J., and Matsuno-Yagi, A. (1992) in Adenine Nucleotides in Cellular Energy Transfer and Signal Transduction (Papa, S., Azzi, A., and Tager, J., Eds.), pp. 33-46, Birhauser Verlag, Basel, Switzerland.
5. Cross, R., and Nalin, C. (1982) J. Biol. Chem. 257, 2874-2881.
6. Walker, J., Saraste, M., Runswick, M., and Gay, N. (1982) EMBO J. 1, 945-951.
7. Noumi, T., Mosher, M., Natori, S., Futai, M., and Kanazawa, H. (1984) J. Biol. Chem. 259, 10071-10075.
8. Parsonage, D., Duncan, T., Wilkes-Mounts, S., Kironde, F., Hatch, L., and Senior, A. (1987) J. Biol. Chem. 262, 6301-6307.
9. Kironde, F., Parsonage, D., and Senior, A. (1989) Biochem. J. 259, 421-426.
10. Mueller, D. M. (1989a) J. Biol. Chem. 264, 16552-16556.
11. Mueller, D. M. (1989b) Biochem. Biophys. Res. Commun. 164, 381-386.
12. Garboczi, D., Thomas, P., and Pedersen, P. (1990) J. Biol. Chem. 265, 14632-14637.
13. Miki, J., Fujiwara, K., Tsuda, M., Tsuchiya, T., and Kanazawa, H. (1990) J. Biol. Chem. 265, 21567-21572.
14. Takeyama, M., Ihara, K., Moriyama, Y., Noumi, T., Ida, K., Tomioka, N., Itai, A., Maeda, M., and Futai, M. (1990) J. Biol. Chem. 265, 21279-21284.
15. Lee, R., Pagan, J., Wilkes-Mounts, S., and Senior, A. (1991) Biochemistry 30, 6842-6847.
16. Futai, M., Iwamoto, A., Omote, H., and Maeda, M. (1992) J. Bioenerg. Biomembr. 24, 463-467.
17. Omote, H., Maeda, M., and Futai, M. (1992) J. Biol. Chem. 267, 20571-20576.
18. Senior, A., and Al Shawi, M. (1992) J. Biol. Chem. 267, 21471-21478.
19. Thomas, P., Garboczi, D., and Pedersen, P. (1992) J. Biol. Chem. 267, 20331-20338.
20. Shen, H., Yao, B. Y., and Mueller, D. M. (1994) J. Biol. Chem. 269, 9424-9428.
21. Garboczi, D., Shenbagamurthi, P., Kirk, W., Hullihen, J., and Pedersen, P. (1988) J. Biol. Chem. 263, 812-816.
22. Pai, F., Sachsenheimer, W., Schirmer, R., and Schulz, G. (1977) J. Mol. Biol. 114, 37-45.
23. Fry, D., Kuby, S., and Mildvan, A. (1985) Biochemistry 24, 4680-4694.
24. Tian, G., Sanders, C., Kishi, F., Nakazawa, A., and Tsai, M.-D. (1988) Biochemistry 27, 5544-5552.
25. Abraham, J. P., Leslie, A. G. W., Lutter, R., and Walker, J. E. (1994) Nature 370, 621-628.
26. Hanahan, D. (1983) J. Mol. Biol. 166, 557-580.
27. Ito, H., Fukada, Y., Murata, K., and Kimura, A. (1983) J. Bacteriol. 153, 163-168.
28. Hinnen, A., Hicks, J. B., and Fink, G. R. (1978) Proc. Natl. Acad. Sci. USA 75, 1929-1933.
29. Vernet, T., Dignard, D., and Thomas, D. (1987) Gene 52, 225-233.
30. Morinaga, Y. T., Franceschini, T., Inouye, S., and Inouye, M. (1984) Bio/Technology 5, 636-639.
31. Mueller, D. M. (1988) J. Biol. Chem. 263, 5634-5639.
32. Rott, R., and Nelson, N. (1981) J. Biol. Chem. 256, 9224-9228.
33. Ebel, R., and Lardy, H. (1975) J. Biol. Chem. 250, 191-196.
34. Henderson, P. F. (1972) Biochem. J. 127, 321-333.
35. Cleland, W. (1979) in Methods of Enzymology (Purich, D., Ed.), Vol. 63, pp. 103-138, Academic Press, New York.
36. Maniatis, T., Fritsch, E., and Sambrooke, J. (1982) Molecular Cloning, A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
37. McClellan, D., and Tzagoloff, A. (1968) Biochemistry 7, 1603-1610.
38. Uh, M., Jones, D., and Mueller, D. (1990) J. Biol. Chem. 265, 19047-19052.
39. Guelin, E., Chevallier, J., Rigoulet, M., Guerin, B., and Velours, J. (1993) J. Biol. Chem. 268, 161-167.
40. Kumamoto, C., and Simoni, R. (1986) J. Biol. Chem. 261, 10037-10042.
41. Kumamoto, C., and Simoni, R. (1987) J. Biol. Chem. 262, 3060-3064.
42. Cain, B., and Simoni, R. (1988) J. Biol. Chem. 263, 6606-6612.
43. Nakamoto, R., Maeda, M., and Futai, M. (1993) J. Biol. Chem. 268, 867-872.
44. Iwamoto, A., Omote, H., Hanada, H., Toioka, N., Itai, A., Maeda, M., and Futai, M. (1991) J. Biol. Chem. 266, 16350-16355.
45. Miki, J., Tsugumi, S., Ikeda, H., and Kanazawa, H. (1994) FEBS Lett. 187-190.
46. Dunn, S., and Heppel, L. A. (1981) Arch. Biochem. Biophys. 210, 421-436.
47. Klionsky, D., and Simoni, R. (1985) J. Biol. Chem. 260, 11200-11206.
48. Duncan, T., Parsonage, D., and Senior, A. (1986) FEBS Lett. 208, 1-6.
49. Fillingame, R. (1990) in The Bacteria: A Treatise on Structure and Function. Volume XII. Bacterial Energetics (Krulivich, T., Ed.), pp. 345-391, Academic Press, New York.
50. Fry, D., Kuby, S., and Mildvan, A. (1987) Biochemistry 26, 1645-1655.