Abstract
MUTATIONS of the Drosophila melanogaster ninaA gene affect phototransduction: ninaA mutant flies have a 10-fold reduction in the levels of rhodopsin in the R1–R6 photoreceptor cells1,2. The ninaA gene was isolated and found to encode a 237-amino-acid protein that has over 40% amino-acid sequence identity with the vertebrate cyclosporin A-binding protein, cyclophilin, a protein that seems to be involved in T-lymphocyte activation. The remarkable evolutionary conservation of cyclophilin in two phylogeneti-cally distant organisms and its involvement in diverse transduction processes suggests that this protein plays an important role in cellular metabolism. Indeed, cyclophilin has recently been shown to be a prolyl cis–trans isomerase that catalyses, in vitro, rate-limiting steps in the folding of a number of proteins3,23. Here, we present evidence for the involvement of cyclophilin-like molecules in a defined cellular process. The availability of mutations in a cyclophilin gene provides a new model system for the study of cyclophilin and cyclosporin action.
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References
Larrivee, D. C., Conrad, S. Stepheson, R. S. & Pak, W. L. J. gen. Physiol. 78, 521–545 (1981).
Stephenson, R. S., O'Tousa, J., Scavarda, N. J., Randall, L. L. & Pak, W. L. in The Biology of Photoreception (eds Cosens, D. J. & Vince-Price, D.), 477–501 (Cambridge University Press, 1983).
Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T. & Schmid, F. X. Nature 337, 476–481 (1989).
Hall, J. C. Q. Rev. Biophys. 15, 223–479 (1982).
Heisenberg, M. & Wolf, R. in Vision in Drosophila: Genetics of Microbehavior, Studies of Brain Function Vol. 12 (ed. Braitenberg, V). (Springer, Berlin, 1984).
Zuker, C. S., Mismer, D., Hardy, R. & Rubin, G. M. Cell 53, 475–485 (1988).
Sved, J. Drosoph. Info. Serv. 73, 169 (1986).
Handschumacher, R. E., Harding, M. W., Rice, J., Drugge, R. J. & Speicher, D. W. Science 226, 544–547 (1984).
Merker, M. M. & Handschumacher, R. E. J. Immun. 132, 3064–3070 (1984).
Harding, M. H., Handschumacher, R. E. & Speicher, D. W. J. biol. Chem. 261, 8547–8555 (1986).
Koletsky, A. J., Harding, M. W. & Handschumacher, R. E. J. Immun. 137, 1054–1059 (1986).
Borel, J. F., Feurer, C., Gubler, H. & Stahelin, H. Agents and Actions 6, 468–475 (1976).
Cohen, D. J., et al. Ann. intern. Med. 101, 667–682 (1984).
Shevach, E. M. A. Rev. Immun. 3, 397–423 (1985).
Drugge, R. J. & Handschumacher, R. E. Transplant Proc. 20, Suppl. 2, 301–309 (1988).
Second International Congress on Cydosporine, Transplant Proc. 20, Suppl. 2 (1988).
International Symposium on the Mechanism of Action of Cyclosporine Transplantation 46, 1S (1988).
Manger, B., Hardy, K. J., Weiss, A. & Stobo, J. D. J. clin. Invest. 77, 1501–1506 (1986).
Szamel, M., Berger, P. & Resch, K. J. Immun. 136, 264–269 (1986).
Rosoff, P. M. & Terres, G. J. Cell Biol. 103, 457–463 (1986).
Rubin, G. M. Trends Neurosci. 8, 231–233 (1985).
Rubin, G.M. Science 240, 1452–1459 (1988).
Ostroy, S. E., Wilson, M. & Pak, W. L. Biochem. biophys. Res. Commun. 59, 960–966 (1974).
Davis, M. M. et al. Proc. natn. Acad. Sci. U.S.A. 81, 2194–2198 (1984).
Maniatis, T., Fritsch, E. F. & Sambrook, J. in Molecular Cloning, A Laboratory Manual (Cold Spring Harbor Laboratory, New York, 1982).
Sanger, F., Nicklen, S. & Coulson, A. R., Proc. natn. Acad. Sci. U.S.A. 74, 5463–5467 (1977).
Haendler, B., Hofer-Warbinek, R. & Hofer, E. EMBO J. 6, 947–950 (1987).
Danielson, P. E. et al. DNA 7, 261–267 (1988).
Takahashi, N., Hayano, T. & Suzuki, M. Nature 337, 473–475 (1989).
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Shieh, BH., Stamnes, M., Seavello, S. et al. The ninaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding protein. Nature 338, 67–70 (1989). https://doi.org/10.1038/338067a0
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DOI: https://doi.org/10.1038/338067a0
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