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Bet2p and Mad2p are components of a prenyltransferase that adds geranylgeranyl onto Ypt1p and Sec4p

Naturevolume 366pages8486 (1993) | Download Citation

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Abstract

THREE different prenyltransferases have been identified in yeast and higher cells1–6, the farnesyltransferase and the type I and type II geranylgeranyltransferases (GGTase). The farnesyltransferase and GGTase-I modify peptides in vitro with the CAAX (C, Cys; A, aliphatic residue; X, terminal amino acid) consensus motif2,7. These enzymes are heterodimers that have different β-subunits and a shared α-subunit8. In yeast, the RAM2 gene encodes this α-subunit9. RAM2 is also homologous to MAD2, a yeast gene whose product has been implicated in the feedback control of mitosis10,11. We have shown that Bet2p is a component of the yeast GGTase-II (refs 6,12) that geranylgeranylates Yptlp, a small GTP-binding protein that mediates transport from the endoplasmic reticulum to the Golgi complex13–15. Here we report that Mad2p is a component of this enzyme. Bet2p forms a complex with Mad2p that appears to bind geranylgeranyl pyrophosphate, but not farnesyl pyrophosphate. The efficient transfer of geranylgeranyl onto small GTP-binding proteins requires the presence of an additional activity.

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References

  1. 1

    Reiss, Y., Goldstein, J. L., Seabra, M. C., Casey, P. J. & Brown, M. S. Cell 62, 81–88 (1990).

  2. 2

    Moores, S. L. et al. J. biol. Chem. 266, 14603–14610 (1991).

  3. 3

    Moomaw, J. F. & Casey, P. J. J. biol. Chem. 267, 17438–17443 (1992).

  4. 4

    Schafer, W. R. et al. Science 249, 1133–1139 (1990).

  5. 5

    Finegold, A. A. et al. Proc. natn. Acad. Sci. U.S.A. 88, 4448–4452 (1991).

  6. 6

    Kohl, N. E. et al. J. biol. Chem. 266, 18884–18888 (1991).

  7. 7

    Reiss, Y., Stradley, S. J., Gierasch, L. M., Brown, M. S. & Goldstein, J. L. Proc. natn. Acad. Sci. U.S.A. 88, 732–736 (1991).

  8. 8

    Seabra, M. C. Reiss, Y., Casey, P. J., Brown, M. S. & Goldstein, J. L. Cell 65, 429–434 (1991).

  9. 9

    He, B. et al. Proc. natn. Acad. Sci. U.S.A. 88, 11373–11377 (1991).

  10. 10

    Li, R. & Murray, A. Cell 66, 519–531 (1991).

  11. 11

    Boguski, M. S., Murray, A. W. & Powers, S. New Biol. 4, 1–4 (1992).

  12. 12

    Rossi, G., Jiang, Y., Newman, A. P. & Ferro-Novick, S. Nature 351, 158–161 (1991).

  13. 13

    Segev, N., Mulholland, J. & Botstein, D. Cell 52, 915–924 (1988).

  14. 14

    Bacon, R. A., Salminen, A., Ruohola, H., Novick, P. & Ferro-Novick, S. J. Cell Biol. 109, 1015–1022 (1989).

  15. 15

    Baker, D., Wuestehube, L., Schekman, R., Botstein, D. & Segev, N. Proc. natn. Acad. Sci. U.S.A. 87, 355–359 (1990).

  16. 16

    Salminen, A. & Novick, P. Cell 49, 527–538 (1987).

  17. 17

    Seabra, M. C., Goldstein, J., Sudhof, T. C. & Brown, M. S. J. biol. Chem. 267, 14497–14503 (1992).

  18. 18

    Seabra, M. C., Brown, M. S., Slaughter, C. A., Sudhof, T. C. & Goldstein, J. L. Cell 70, 1049–1057 (1992).

  19. 19

    Kinsella, B. & Maltese, W. A. J. biol. Chem. 266, 8540–8544 (1991).

  20. 20

    Mayer, M. L., Caplin, B. E. & Marshall, M. S. J. biol. Chem. 267, 20589–20593 (1992).

  21. 21

    Newman, A. & Ferro-Novick, S. J. Cell Biol. 105, 1587–1594 (1987).

  22. 22

    Li, R., Havel, C., Watson, J. A. & Murray, A. W. Nature 366, 82–84 (1993).

  23. 23

    Andres, D. A. et al. Cell 73, 1091–1099 (1993).

  24. 24

    Araki, S., Kikuchi, A., Hata, Y., Isomura, M. & Takai, Y. J. biol. Chem. 265, 13007–13015 (1990).

  25. 25

    Armstrong, S. A., Seabra, M. C., Sudhof, T. C., Goldstein, J. L. & Brown, M. S. J. biol. Chem. 268, 12221–12229 (1993).

  26. 26

    Wagner, P. et al. EMBO J. 6, 2373–2379 (1987).

  27. 27

    Walworth, N. C., Brennwald, P., Kabcenell, A. K., Garrett, M. & Novick, P. Molec. cell. Biol. 12, 2017–2028 (1992).

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  1. Susan Ferro-Novick: To whom correspondence should be addressed.

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  1. Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut, 06510, USA

    • Yu Jiang
    • , Guendalina Rossi
    •  & Susan Ferro-Novick

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https://doi.org/10.1038/366084a0

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