Protein isoprenylation in plants

Critical Reviews in Biochemistry and Molecular Biology

Volumn 34, Issue 5, 1999, Pages 325-338

  Randall, Stephen K ^a   Crowell, Dring N ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; GERANYLTRANSFERASE; GUANINE NUCLEOTIDE BINDING PROTEIN; ISOPRENOID; MEVALONIC ACID; PROTEIN FARNESYLTRANSFERASE;

BIOSYNTHESIS; CELL GROWTH; CYTOSKELETON; ISOPRENYLATION; MAMMAL CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN MODIFICATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; REVIEW; SIGNAL TRANSDUCTION; YEAST CELL;

ANIMALS; FUNGAL PROTEINS; HYDROXYMETHYLGLUTARYL COA REDUCTASES; MAMMALS; PHYTOSTEROLS; PLANT PROTEINS; PLANTS; PROTEIN ISOPRENYLATION; PROTEINS;

MAMMALIA;

EID: 0032729678     PISSN: 10409238     EISSN: None     Source Type: Journal    
DOI: 10.1080/10409239991209336     Document Type: Review

References (192)

1. Heftmann, E., Functions of steroids in plants, Phytochemistry, 14, 891, 1975.
2. Heftmann, E., Biogenesis of steroids in Solanaceae, Phytochemistry, 22, 1843, 1983.
3. Bach, T. J. and Lichtenthaler, H. K., Inhibition by mevinolin of plant growth, sterol formation and pigment accumulation, Physiol. Plant., 59, 50, 1983.
4. Bach, T. J., Hydroxymethylglutaryl-CoA reductase, a key enzyme in phytosterol synthesis? Lipids, 21, 82, 1986.
5. Bach, T. J., Synthesis and metabolism of mevalonic acid in plants, Plant Physiol. Biochem., 25, 163, 1987.
6. Mok, D.W.S. and Mok, M. C., Cytokinins: Chemistry, Activity, and Function, CRC Press, Boca Raton, FL, 1994.
7. Croteau, R., Biosynthesis of monoterpenes, in Biosynthesis of Isoprenoid Compounds, Vol. I, Porter, J. W. and Spurgeon, S. L., Eds., John Wiley & Sons, New York, 1981, 225.
8. 14C from acetate and mevalonate into rishitin and steroid glycoalkaloids by potalo tuber slices inoculated with Phytophthora infestans, Phytopathology, 63, 826, 1973.
9. Kuc, J. and Lisker, N., Terpenoids and their role in wounded and infected plant storage tissue, in Biochemistry of Wounded Plant Tissues, Kahl, G., Ed., Walter de Gruyter, New York, 1978, 203.
10. Kuc, J. and Rush, J. S., Phytoalexins, Arch. Biochem. Biophys., 236, 455, 1985.
11. Oba, K., Kondo, K., Doke, N., and Uritani, I., Induction of 3-hydroxy-3-methylglutaryl CoA reductase in potato tubers after slicing, fungal infection or chemical treatment, and some properties of the enzyme, Plant Cell Physiol., 26, 973, 1985.
12. Stermer, B. A. and Bostock, R. M., Involvement of 3-hydroxy-3-methylglutaryl coenzyme A reductase in the regulation of sesquiterpenoid phytoalexin synthesis in potato, Plant Phyiol., 84, 404, 1987.
13. Brown, M. S. and Goldstein, J. L., Multivalent feedback regulation of HMG CoA reductase, a control mechanism coordinating isoprenoid synthesis and cell growth, J. Lipid Res., 21, 505, 1980.
14. Goldstein, J. L. and Brown, M. S., Regulation of the mevalonate pathway, Nature, 343, 425, 1990.
15. Swiezewska, E., Dallner, G., Andersson, B., and Ernster, L., Biosynthesis of ubiquinone and plastoquinone in the endoplasmic reticulum-Golgi membranes of spinach leaves, J. Biol. Chem., 268, 1494, 1993.
16. Trebst, A., Plastoquinones in photosynthesis, Philos. Trans. R. Soc. London Ser. B, 284, 501, 1978.
17. Tjamos, E. C. and Kuc, J. A., Inhibition of steroid glycoalkaloid accumulation by arachidonic and elcosapentaenoic acids in potato, Science, 217, 542, 1982.
18. Cutler, H. G., Yokota, T., and Adam, G., Brassinosteroids: Chemistry, Bioactivity, and Applications, American Chemical Society, Washington, D.C., 1991.
19. Crozler, A., Aspects of the metabolism and physiology of gibberellins, in Advances in Botanical Research, Woolhouse, H. W., Ed., Academic Press, New York, 1981, 33.
20. Crozier, A., The Biochemistry and Physiology of Gibberellins, Vols. 1 and 2, Praeger Publishers, New York, 1983.
21. Goodwin, T. W., The Biochemistry of the Carotenoids, Vol. 1, 2nd ed., Methuen, New York, 1980.
22. Parry, A. D. and Horgan, R., Carotenoids and abscisic acid (ABA) biosynthesis in higher plants. Physiol. Plant., 82, 320, 1991.
23. Brown, J. S., Forms of chlorophyll in vivo, Annu. Rev. Plant Physiol., 23, 73, 1972.
24. Shih, M., Kuc, J., and Williams, E. B., Suppression of steroid glycoalkaloid accumulation as related to rishitin accumulation in potato tubers, Phytopathology, 63, 821, 1973.
25. Chappell, J. and Nable, R., Induction of sequiterpenoid biosynthesis in tobacco cell suspension cultures by fungal elicitor, Plant Physiol., 85, 469, 1987.
26. Threlfall, D. R. and Whitehead, I. M., Co-ordinated inhibition of squalene synthetase and induction of enzymes of sesquiterpenoid phytoalexin biosynthesis in cultures of Nicotiana tabacum, Phytochemistry, 27, 2567, 1988.
27. Vögeli, U. and Chappell, J., Induction of sesquiterpene eyelase and suppression of squalene synthetase activities in plant cell cultures treated with fungal elicitor, Plant Physiol., 88, 1291, 1988.
28. Zook, M. N. and Kuc, J. A., Induction of sesquiterpene eyelase and suppression of squalene synthetase activity in elicitor-treated or fungal-infected potalo tuber tissue. Physiol. Mol. Plant Pathol., 39, 377, 1991.
29. Threlfall, D. R. and Whitehead, I. M., Redirection of terpenoid biosynthesis in elicitor-treated plant cell suspension cultures, in Plant Lipid Biochemistry, Structure and Utilization, Quinn, P. J. and Harwood, J. L., Eds., Portland Press. London, 1990, 344.
30. Yang, Z., Park, H., Lacy, G. H., and Cramer, C. L., Differential activation of potalo 3-hydroxy-3-methylglutaryl coenzyme A reductase genes by wounding and pathogen challenge, Plant Cell, 3, 397, 1991.
31. Choi, D., Ward, B. L., and Bostock, R. M., Differential induction and suppression of potato 3-hydroxy-3-methylglutaryl coenzyme A reductase genes in response to Phytophthora infestans and to its elicitor arachidonic acid, Plant Cell, 4, 1333, 1992.
32. Bach, T. J. and Lichtenthaler, H. K., Mevinotin: A highly specific inhibitor of microsomal 3-hydroxy-3-methylglutaryl-coenzyme A reductase of radish plants, Z. Naturforsch., 37c, 46, 1982.
33. Hashizume, T., Matsubara, S., and Endo, A., Compactin (ML-236B) as a new growth inhibitor of plant callus, Agric. Biol. Chem., 47, 1401, 1983.
34. Hata, S., Takagishi, H., and Kouchi, H., Variation in the content and composition of sterols in alfalfa seedlings treated with compactin (ML-236B) and mevalonic acid, Plant Cell Physiol., 28, 709, 1987.
35. Gondet, L., Weber, T., Maillot-Vernier, P., Benveniste, P., and Bach, T. J., Regulatory role of microsomal 3-hydroxy-3-methylglutaryl-coenzyme A reductase in a tobacco mutant that overproduces sterols, Biochem. Biophys. Res, Commun., 186, 888, 1992.
36. Maltese, W. A., Posttranslational modification of proteins by isoprenoids in mammalian cells, FASEB J., 4, 3319, 1990.
37. Casey, P. J., Biochemistry of protein prenylation, J. Lipid Res., 33, 1731, 1992.
38. Clarke, S., Protein isoprenylation and methylation at carboxyl-terminal cysteine residues, Annu. Rev. Biochem., 61, 355, 1992.
39. Schafer, W. R., and Rine, J., Protein prenylation: Genes, enzymes, targets, and functions, Annu. Rev. Genet., 30, 209, 1992.
40. Sinensky, M. and Lutz, R. J., The prenylation of proteins, BioEssays, 14, 25, 1992.
41. Maltese, W. A. and Sheridan, K. M., Differentiation of neuroblastoma cells induced by an inhibitor of mevalonate synthesis: Relation of neurite outgrowth and acetylcholinesterase activity to changes in cell proliferation and blocked isoprenoid synthesis, J. Cell. Physiol., 125, 5440, 1985.
42. Maltese, W. A. and Sheridan, K. M., Isoprenylated proteins in cultured cells: Subcellular distribution and changes related to altered morphology and growth arrest induced by mevalonate deprivation, J. Cell. Physiol., 133, 471, 1987.
43. Schmidt, R. A., Schneider, C. J., and Glomset, J. A., Evidence for post-translational incorporation of a product of mevalonic acid into Swiss 3T3 cell proteins, J. Biol. Chem., 259, 10175, 1984.
44. Hancock, J. F., Magee, A. I., Childs, J. E., and Marshall, C. J., All ras proteins are polyisoprenylated but only some are palmitoylated, Cell, 57, 1167, 1989.
45. Maltese, W. A. and Erdman, R. A., Characterization of isoprenoid involved in the post-translational modification of mammalian cell proteins, J. Biol. Chem., 264, 18168, 1989.
46. Farnsworth, C. C., Gelb, M. H., and Glomset, J. A., Identification of geranylgeranyl-modified proteins in HeLa cells, Science, 247, 320, 1990.
47. ras farnesyl:protein transferase by Cys-AAX tetrapeptides, Cell, 62, 81, 1990.
48. Rilling, H. C., Breunger, E., Epstein, W. W., and Crain, P. F., Prenylaled proteins: The structure of the isoprenoid group, Science, 247, 318, 1990.
49. Epstein, W. W., Lever, D., Leining, L. M., Bruenger, E., and Rilling, H. C., Quantitation of prenylcysteines by a selective cleavage reaction, Proc. Natl. Acad. Sci. U.S.A., 88, 9668, 1991.
50. Schafer, W. R., Kim, R., Sterne, R., Thorner, J., Kim, S.-H., and Rine, J., Genetic and pharmacological suppression of oncogenic mutations in RAS genes of yeast and humans, Science, 245, 379, 1989.
51. Schafer, W. R., Trueblood, C. E., Yang, C.-C., Mayer, M. P., Rosenberg, S., Poulter, C. D., Kim, S.-H., and Rine, J., Enzymatic coupling of cholesterol intermediates to a mating pheromone precursor and to the Ras protein, Science, 249, 1133, 1990.
52. Clarke, S., Vogel, J. P., Deschenes, R. J., and Stock, J., Posttranslational modification of the Ha-ras oncogene protein: Evidence for a third class of protein carboxyl methyltransferases, Proc. Natl. Acad. Sci U.S.A., 85, 4643, 1988.
53. ras is two-step and involves carboxyl-methylation and carboxy-terminal proteolysis, EMBO J, 8, 1093, 1989.
54. Manne, V., Roberts, D., Tobin, A., O'Rourke, E., De Virgilio, M., Meyers, C., Ahmed, N., Kurz, B., Resh, M., Kung, H.-F., and Barbacid, M., Identification and preliminary characterization of protein-cysteine farnesyltransferase, Proc. Natl. Acad. Sci. U.S.A., 87, 7541, 1990.
55. Schaber, M. D., O'Hara, M. B., Garsky, V. M., Mosser, S. D., Bergstrom, J. D., Moores, S. L., Marshall, M. S., Friedman, P. A., Dixon, R. A. F., and Gibbs, J. B., Polyisoprenylation of Ras in vitro by a farnesyl-protein transferase, J. Biol. Chem., 265, 14701, 1990.
56. Hrycyna, C. A. and Clarke, S., Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in Saccharomyces cerevisiae, Mol. Cell. Biol., 10, 5071, 1990.
57. Stephenson, R. C. and Clarke, S., Identification of a C-terminal protein carboxyl methyltransferase in rat liver membranes utilizing a synthetic farnesyl cysteine-containing peptide substrate, J. Biol. Chem., 265, 16248, 1990,
58. K-rasB, EMBO J., 10, 641, 1991.
59. Hrycyna, C. A., Sapperstein, S. K., Clarke, S., and Michaelis, S., The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins, EMBO J., 10, 1699, 1991.
60. Marcus, S., Caldwell, G. A., Miller, D., Xue, C.-B., Naider, F., and Becker, J. M., Significance of C-terminal cysteine modifications to the biological activity of the Saccharomyces cerevisiae a-factor mating pheromone, Mol. Cell. Biol., 11, 3603, 1991.
61. Volker, C., Lane, P., Kwee, C., Johnson, M., and Stock, J., A single activity carboxyl methylates both farnesyl and gernylgeranyl cysteine residues, FEBS Lett., 295, 189, 1991.
62. Ashby, M. N., King, D. S., and Rine, J., Endoproteolytic processing of a farnesylated peptide in vitro, Proc. Natl. Acad. Sci. U.S.A., 89, 4613, 1992.
63. Hrycyna, C. A. and Clarke, S., Maturation of isoprenylated proteins in Saccharomyces cerevisiae: Multiple activities catalyze the cleavage of the three carboxyl-terminal amino acids from farnesylated substrates in vitro, J. Biol. Chem., 267, 10457, 1992.
64. Sapperstein, S., Berkower, C., and Michaelis, S., Nucleotide sequence of the yeast STE14 gene, which encodes farnesylcysteine carboxyl methyltransferase, and demonstration of its essential role in a-factor export, Mol. Cell. Biol., 14, 1438, 1994.
65. Casey, P. J., Thissen, J. A., and Moomaw, J. F., Enzymatic modification of proteins with a geranylgeranyl isoprenoid, Proc. Natl. Acad. Sci. U.S.A., 88, 8631, 1991.
66. Kohl, N. E., Diehl, R. E., Schaber, M. D., Rands, E., Soderman, D. D., He, B., Moores, S. L., Pompliano, D. L., Ferro-Novick, S., Powers, S., Thomas, K. A., and Gibbs, J. B., Structural homology among mammalian and Saccharomyces cerevisiae isoprenyl-protein transferases, J. Biol. Chem., 266, 18884, 1991.
67. Moores, S. L., Schaber, M. D., Mosser, S. D., Rands, E., O'Hara, M. B., Garsky, V. M., Marshall, M. S., Pompliano, D. L., and Gibbs, J. B., Sequence dependence of protein isoprenylation, J. Biol. Chem., 266, 14603, 1991.
68. Seabra, M. C., Guldstein, J. L., Südhof, T. C., and Brown, M. S., Rab geranylgeranyl transferase: A multisubunit enzyme that prenylates GTP-binding proteins terminating in Cys-X-Cys or Cys-Cys, J. Biol. Chem., 267, 14497, 1992.
69. H ras farnesyltransferase: Peptide binding and farnesyl pyrophosphate carrier functions, J. Biol. Chem., 266, 10672, 1991.
70. Seabra, M. C., Reiss, Y., Casey, P. J., Brown, M. S., and Goldstein, J. L., Protein farnesyltransferase and geranylgeranyltransferase share a common α subunit, Cell, 65, 429, 1991.
71. Mayer, M. L., Caplin, B. E., and Marshall, M. S., CDC43 and RAM2 encode the polypeptide subunits of a yeast type I protein geranylgeranyltransferase, J. Biol. Chem., 267, 20589, 1992.
72. Andres, D. A., Seabra, M. C., Brown, M. S., Armstrong, S. A., Smeland, T. E., Cremers, F. P. M., and Goldstein, J. L., cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein, Cell, 73, 1091, 1993.
73. Jiang, Y., Rossi, G., and Ferro-Novick, S., Bet2p and Mad2p are components of a prenyltransferase that adds geranylgeranyl onto Ypt1p and Sec4p, Nature, 366, 84, 1993.
74. Li, R., Havel, C., Watson, J. A., and Murray, A. W., The mitotic feedback contronl gene MAD2 encodcs the asubunit of a prenyltransferase, Nature, 366, 82, 1993.
75. Jiang, Y. and Ferro-Novicik, S., Idenification of yeast component A: Reconsitution of the geranylgcranyltransferase that modifies Ypt1p and Sec4p, Proc. Natl. Acad. Sci. U.S.A., 91, 4377, 1994.
76. Seabra, M. C., Brown, M. S., Slaughter, C. A., Südhof, T. C., and Goldstein, J. L., Purification of component A of Rab geranylgeranyl transferase: Possible identity with the choroidcremia gene product, Cell, 70, 1049, 1992.
77. Kamiya, Y., Sakurai, A., Tamura, S., Takahashi, N., Tsuchiya, E., Abe, K., and Fukui, S., Structure of rhodotorucine A, a peptidyl factor, inducing mating tube formation in Rhodosporidium toruloides, Agric. Biol. Chem., 43. 363, 1979.
78. Anderegg, R. J., Betz, R., Carr, S. A., Crabb, J. W., and Duntze, W., Structure of Saccharomyces cerevisiae mating hormone a-factor: Identification of S-farnesyl cysteine as a structural component, J. Biol. Chem., 263, 18236, 1988.
79. Casey, P. J., Selski, P. A., Der, C. J., and Buss, J. E., p21ras is modified by a farnesyl isoprenoid, Proc. Natl. Acad. Sci. U.S.A., 86, 8323, 1989.
80. Didsbury, J. R., Uhing, R. J., and Snyderman, R., Isoprenylation of the low molecular mass GTP-binding proteins RAC1 and RAC2: Possible role in membrane localization, Biochem. Biophys. Res. Commun., 171, 804, 1990.
81. Jackson, J. H., Cochrane, C. G., Bourne, J. R., Solski, P. A., Buss, J. E., and Der, C. J., Farnesol modification of Kirsten-ras exon 4B protein is essential for transformation, Proc. Natl. Acad. Sci. U.S.A., 87, 3042, 1990.
82. Kawata, M., Farnsworth, C. C., Yoshida, Y., Gelb, M. H., Glomset, J. A., and Takai, Y., Posttranslationally processed structure of the human platelet protein smg p21B: Evidente for geranylgeranylation and carboxyl methylation of the C-terminal cysteine, Proc. Natl. Acad. Sci. U.S.A., 87, 8960, 1990.
83. ras, J. Biol. Chem., 265, 5157, 1990.
84. ras, J. Biol. Chem., 265, 17883, 1990.
85. Maltese, W. A., Sheridan, K. M., Repko, E. M., and Erdman, R. A., Post-translational modification of low molecular mass GTP-binding proteins by isoprenoid, J. Biol. Chem., 265, 2148, 1990.
86. Khosravi-Far, R., Lutz, R. J., Cox, A. D., Conroy, L., Bourne, J. R., Sinensky, M., Balch, W. E., Buss, J. E., and Der, C. J., Isoprenoid modification of rab proteins terminating in CC or CXC motifs, Proc. Natl. Acad. Sci. U.S.A., 88, 6264, 1991.
87. Kinsella, B. T., Erdman, R. A., and Maltese, W. A., Posttranslational modification of Ha-ras p21 hy farnesyl versus geranylgeranyl isoprenoids is determined by the COOH-terminal amino acid, Proc. Natl. Acad. Sci U.S.A., 88, 8934, 1991.
88. Kinsella, B. T., Erdman, R. A., and Maltese, W. A., Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA, J. Biol. Chem., 266, 9786, 1991.
89. Winegar, D. A., Molina y Vedia, L., and Lapetina, E. G., Isoprenylation of rap2 proteins in platelets and human erythroleukumia cells, J. Biol. Chem., 266, 4381, 1991.
90. Kinsella, B. T. and Maltese, W. A., rab GTP-binding proteins with three differcnt carboxyl-terminal cysteine motits are modifed in vivo by 20-carbon isoprenoids, J. Biol. Chem., 267, 3940, 1992.
91. tab2, a ras-like GTPase with a -GGGCC C-terminus, is isoprenylated but not detectably carboxymethylated in N1H3T3 cells, Oncogene, 7, 467, 1992.
92. Finegold, A. A., Schafer, W. R., Rine, J., Whiteway, M., and Tamanoi, F., Common modifications of trimeric G proteins and ras protein: Involvement of polyisoprenylation, Science, 249, 165, 1990.
93. Fukada, Y., Takao, T, Ohguro, H., Yoshizawa, T., Akino, T., and Shimonishi, Y., Farnesylated γ-subunit of photoreceptor G protein indispensable for GTP-binding, Nature, 346, 658, 1990.
94. Maltese, W. A. and Robishaw, J. D., Isoprenylation of C-terminal cyslcine in a G-protcin γ subunit, J. Biol. Chem., 265, 18071, 1990.
95. Mumby, S, M., Casey, P. J., Gilman, A. G., Gutowski, S., and Sternweis, P. C., G protein γ subunits contain a 20-carbon isoprenoid, Proc. Natl. Acad. Sci. U.S.A., 87, 5873, 1990.
96. Yamane, H. K., Farnsworth, C. C., Xie, H., Howald, W., Fung, B. K.-K., Clarke, S., Gelb, M. H., and Glomset, J. A., Brain G protein γ subunits contain an all-trans-geranylgeranyl-cysteine methyl ester at their carboxyl termini, Proc. Natl. Acad. Sci. U.S.A., 87, 5868, 1990.
97. Wolda, S. L. and Glomset, J. A., Evidente for modification of lamin B by a product of mevalonic acid, J. Biol. Chem., 263, 5997, 1988.
98. Farnsworth, C. C., Wolda, S. L., Gelb, M. H., and Glomset, J. A., Human lamin B contains a farnesylated cysteine residue, J. Biol. Chem., 264, 20422, 1989.
99. Vorhurger, K., Kitten, G. T., and Nigg, E. A., Modification of nuclear lamin proteins by a mevalonic acid derivative occurs in reticulocyte lysates and requires the cysteine residue of the C-terminal CXXM motif, EMBO J., 8, 4007, 1989.
100. Lutz, R. J., Trujillo, M. A., Denham, K. S., Wenger, L., and Sinensky, M., Nucleoplasmic localization of prelamin A: Implications for prenylation-dependent lamin A assembly into the nuclear lamina, Proc. Natl. Acad. Sci. U.S.A., 89, 3000, 1992.
101. Hennekes, H. and Nigg, E. A., The role of isoprenylation in membrane attachment of nuclear lamins: A single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties, J. Cell Sci., 107, 1019, 1994.
102. Sinensky, M., Fantle, K., Trujillo, M., McLain, T., Kupfer, A., and Dalton, M., The processing pathway of prelamin A, J. Cell Sci., 107, 61, 1994.
103. Heilmeyer, L. M. G., Jr., Serwe, M., Weber, C., Metzger, J., Hoffmann-Posorske, E., and Meyer, H. E., Farnesylcysteine, a constituent of the α and β subunits of rabbit skeletal muscle phosphorylase kinase: Localization by conversion to S-ethylcysteine and by tandem mass spectrometry, Proc. Natl. Acad. Sci. U.S.A, 89, 9554, 1992.
104. Inglese, J., Glickman, J. F., Lorenz, W., Caron, M. G., and Lefkowitz, R. J., Isoprenylation of a protein kinase: Requirement of farnesylation/α-carboxyl methylation for full enzymatic activity of rhodopsin kinase, J. Biol Chem., 267, 1422, 1992.
105. Inglese, J., Koch, W. J., Caron, M. G., and Lefkowitz, R. J., Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases, Nature, 359, 147, 1992.
106. Vaneura, A., Sessler, A., Leiehus, B., and Kuret, J., A prenylation motif is required for plasma membrane localization and biochemical function of casein kinase I in budding yeast, J. Biol. Chem., 269, 19271, 1994.
107. Braun, P. E., De Angelis, D., Shtybel, W. W., and Bernier, L., Isoprenoid modification permits 2′,3′-cyclic nucleotide 3′-phosphodiesterase to bind to membranes, J. Neurosci. Res., 30, 540, 1991.
108. Anant, J. S., Ong, O. C., Xie, H., Clarke, S., O'Brien, P. J., and Fung, B. K.-K., In vivo differential prenylation of retinal cyclic GMP phosphodiesterase catalytic subunits, J. Biol. Chem., 267, 687, 1992.
109. Caplan, A. J., Tsai, J., Casey, P. J., and Douglas, M. G., Farnesylation of YDJ1p is required for function at elevated growth temperatures in Saccharomyces cerevisiae, J. Biol. Chem., 267, 18890, 1992.
110. Cyr, D. M., Lunger, T., and Douglas, M. G., DnaJ-like proteins: Molecular chaperones and specific regulators of 11sp70, Trends Biochem. Sci., 19, 176, 1994.
111. Kloc, M., Reddy, B., Crawford, S., and Etkin, L. D., A novel 110-kDa maternal CAAX box-containing protein from Xenopus is palmitoylated and isoprenylated when expressed in baculovirus, J. Biol. Chem., 266, 8206, 1991.
112. Glenn, J. S., Watson, J. A., Havel, C. M., and White, J. M., Identification of a prenylation site in delta virus large antigen, Science, 256, 1331, 1992.
113. Asundi, V. K., Stahl, R. C., Showalter, L., Conner, K. J., and Carey, D. J., Molecular cloning and characterization of an isoprenylated 67 kDa protein, Biochim. Biophys. Acta, 1217, 257, 1994.
114. James, G. L., Goldstein, J. L., Pathak, R. K., Anderson, R. G. W., and Brown M. S., PxF, a prenylated protein of peroxisomes, J. Biol. Chem., 269, 14182, 1994.
115. Peter, M., Gartner, A., Horecka, J., Ammerer, G., and Herskowitz, I., FAR1 links the signal transduction pathway to the cell cycle machinery in yeast, Cell, 73, 747, 1993.
116. Peter, M. and Herskowitz, I., Direct inhibition of the yeast cyclin-dependent kinase Cdc28-Cln by Far1, Science, 265, 1228, 1994.
117. Qiu, M.-S., Pitts, A. F., Winters, T. R., and Green, S. H., Ras isoprenylation is required for ras-induced bur not for NGF-induced neuronal differentiation of PC12 cells, J. Cell Biol., 115, 795, 1991.
118. Boguski, M. S. and McCormick, F., Proteins regulating Ras and its relatives, Nature, 366, 643, 1993.
119. Lowy, D. R. and Willumsen, B. M., Function and regulation of Ras, Annu. Rev. Biochem., 62, 851, 1993.
120. Crowell, P. L., Chang, R. R., Ren, Z., Elson, C. E., and Gould, M. N., Selective inhibition of isoprenylation of 21-26-kDa proteins by the anticarcinogen d-limonene and its metabolites, J. Biol. Chem., 266, 17679, 1991.
121. Hara, M., Akasaka, K., Aldnaga, S., Okabe, M., Nakano, H., Gomez, R., Wood, D., Uh, M., and Tamanoi, F., Identification of Ras farnesyltransferase inhibitors by microbial screening, Proc. Natl. Acad. Sci. U.S.A., 90, 2281, 1993.
122. James, G. L., Goldstein, J. L., Brown, M. S., Rawson, T. E., Somers, T. C., McDowell, R. S., Crowley, C. W., Lueas, B. K., Levinson, A. D., and Marsters, J. C., Jr., Benzodiazepine peptidomimetics: Potent inhibitors of Ras farnesylation in animal cells, Science, 260, 1937, 1993.
123. Kohl, N. E., Mosser, S. D., deSolms, S. J., Giuliani, E. A., Pompliano, D. L., Graham, S. L., Smith, R. L., Scolnick, E. M., Oliff, A., and Gibbs, J. B., Selective inhibition of ras-dependent transformation by a farnesyltransferase inhibitor, Science, 260, 1934, 1993.
124. Tamanoi, F., Inhibitors of Ras farnesyltransferases, Trends Biochem. Sci., 18, 349, 1993.
125. Cox, A. D., Garcia, A. M., Westwick, J. K., Kowalczyk, J. J., Lewis, M. D., Brenner, D. A., and Der, C. J., The CAAX peptidomimetic compound B581 specifically blocks farnesylated, but not geranylgeranylated or myristylated, oncogenic Ras signaling and transformatioa, J. Biol. Chem., 269, 19203, 1994.
126. Prendergast, G. C., Davide, J. P., deSolms, S. J., Giuliani, E. A., Graham, S. L., Gibbs, J. B., Oliff, A., and Kohl, N. E., Farnesyltransrerase inhibition causes morphological reversion of ras-transformed cells by a complex mechanism that involves regulation of the actin cytoskeleton, Mol. Cell Biol. 14, 4193, 1994.
127. Ohya, Y., Qadota, H., Anraku, Y., Pringle, J. R., and Botstein, D., Suppression of yeast geranylgeranyl transferase I defect by alternative prenylation of two target GTPases, Rho1p and Cdc42p, Mol. Biol. Cell, 4, 1017, 1993.
128. Perona, R., Esteve, P., Jiménez, B., Ballestero, R. P., Ramón y Cajal, S., and Lacal, J. C., Tumorigenic activity of rho genes from Aplysia californica, Oncogene, 8, 1285, 1993.
129. Graham, S. M., Cox, A. D., Drivas, G., Rush, M. G., D'Eustachio, P., and Der, C. J., Aberrant function of the Ras-related protein TC21/R-Ras2 triggers malignant transformation, Mol. Cell. Biol., 14, 4108, 1994.
130. Iñiguez-Lluhi, J. A., Simon, M. I., Robishaw, J. D., and Gilman, A. G., G protein βγ subunits synthesized in St9 cells: Functional characterization and lhe significance of prenylation of γ, J. Biol. Chem., 267, 23409, 1992.
131. Katz, A., Wu, D., and Simon, M. I., Subunits βγ of heterotrimeric G protein activatc β2 isoform of phospholipase C, Nature, 360, 686, 1992.
132. Clapham, D. E., and Neer, E. J., New roles for G-protein βγ-dimers in transmembrane signalling, Nature, 365, 403, 1993.
133. 2 by recombinant guanine-nucleotide-binding protein βγ dimers produced in a baculovirus/insect cell expression system: Requirement of γ-subunit isoprenylation for stimulation of phospholipase C, Eur. J. Biochem., 219, 171, 1994.
134. Stephens, L., Smreka, A., Cooke, F. T., Jackson, T. R., Sternweis, P. C., and Hawkins, P. T., A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein βγ subunits, Cell, 77, 83, 1994.
135. Fenton, R. G., Kung, H.-F., Longo, D. L., and Smith, M. R., Regulation of intracellular actin polymerization by prenylated cellular proteins, J. Cell Biol., 117, 347, 1992.
136. Ridley, A. J. and Hall, A., The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors, Cell, 70, 389, 1992.
137. Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D., and Hall, A., The small GTP-binding protein rac regulares growth factor-induced membrane ruffling, Cell, 70, 401, 1992.
138. Salminen, A. and Novick, P. J., A ras-like protein is required for a post-Golgi event in yeast secretion, Cell, 49, 527, 1987.
139. Goud, B., Salminen, A., Walworth, N. C., and Novick, P. J., A GTP-binding protein required for secretion rapidly associates with secretory vcsicles and the plasma membrane in yeast, Cell, 53, 753, 1988.
140. Balch, W. E., Small GTP-binding proteins in vesicular transport, Trends Biochem. Sci., 15, 473, 1990.
141. Bourne, H. R., Sanders, D. A., and McCormick, F., The GTPase superfamily: A conserved switch for diverse cell functions, Nature, 348, 125, 1990.
142. Chavrier, P., Gorvel, J.-P., Stelzer, E., Simons, K., Gruenberg, J., and Zerial, M., Hypervariable C-terminal domain of rab proteins acts as a targeting signal, Nature, 353, 769, 1991.
143. Rothman, J. E. and Orci, L., Molecular dissection of the secretory pathway, Nature, 355, 409, 1992.
144. Glomset, J. A., Gelb, M. H., and Farnsworth, C. C., Prenyl proteins in eukaryotic cells: A new type of membrane anchor, Trends Biochem. Sci., 15, 139, 1990.
145. Marshall, C. J., Protein prenylation: A mediator of pmtein-protein interactions, Science, 259, 1865, 1993.
146. Kuroda, Y., Suzuki, N., and Kataoka, T., The effect of posttranslational modifications on the interaction of Ras2 with adenylyl cyclase, Science, 259, 683, 1993.
147. Beranger, F., Cadwallader, K., Porfiri, E., Powers, S., Evans, T., de Gunzberg, J., and Hancock, J. F., Determination of structural requirements for the interaction of Rab6 with RabGDI and Rab geranylgeranyltransferase, J. Biol. Chem., 269, 13637, 1994.
148. Kisselev, O. G., Ermolaeva, M. V., and Gautam, N., A farnesylated domain in lhe G protein γ subunit is a specific determinanl of receptor coupling, J. Biol. Chem., 269, 21399, 1994.
149. Porfiri, E., Evans, T., Chardin, P., and Hancock, J. F., Prenylation of Ras Proteins is required for efficient hSOSI-promoted guanine nucleotide exchange, J. Biol. Chem., 269, 22672, 1994.
150. Hwang, S. B. and Lai, M. M. C., Isoprenylation mediates direct protein-protein interactions between hepatitis large delta antigen and hepatitis B viras surface antigen, J. Virol., 67, 7659, 1993.
151. Yang, Z., Cramer, C. L., and Watson, J. C., Protein farnesyltransferase in plants: Molecular cloning and expression of a homolog of the β subunit from the garden pea, Plant Physiol., 101, 667. 1993.
152. Randall, S. K., Marshall, M. S., and Crowell, D. N., Protein isoprenylation in suspension-cultured tobacco cells, Plant Cell, 5, 433, 1993.
153. Crowell, D. N. and Salaz, M. S., Inhibition of growth of cultured tobacco cells at low concentrations of lovastatin is reversed by cytokinin, Plant Physiol., 100, 2090, 1992.
154. Swiezewska, E., Thelin, A., Dallner, G., Andersson, B., and Ernster, L., Occurrence of prenylated proteins in plant cells, Biochem. Biophys. Res. Commun., 192, 161. 1993.
155. Zhu, J.-K., Shi, J., Bressan, R. A., and Hasegawa, P. M., Expression or an Atriplex nummularia gene encoding a protein homologous to the bacterial molecular chaperone DnaJ, Plant Cell, 5, 341, 1993.
156. Zhu, J.-K., Bressan, R. A., and Hasegawa, P. M., Isoprenylation of the plant molecular chaperone ANJ1 facilitates membrane association and function at high temperature, Proc. Natl Acad. Sci. U.S.A., 90, 8557, 1993.
157. Atencio, D. P. and Yaffe, M. P., MAS5, a yeast homolog of DnaJ involved in mitochondrial protein import, Mol. Cell. Biol., 12, 283, 1992.
158. Caplan, A. J., Cyr, D. M., and Douglas, M. G., YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism, Cell, 71, 1143, 1992.
159. Preisig-Müller, R., Muster, G., and Kindl, H., Heat shock enhances the amount of prenylated Dnaj protein at membranes of glyoxysomes, Eur. J. Biochem., 219, 57, 1994.
160. Dillenschneider, M., Hetherington, A., Graziana, A., Alibert, G., Berra, P., Haiech, J., and Ranjeva, R., The formation of inositol phosphate derivatives by isolated membranes from Acer pseudoplatanus is stimulated by guanine nucleotides, FEBS Lett., 208, 413, 1986.
161. Zabulionis, R. B., Atkinson, B. G., Procunier, J. D., and Walden, D. B., Maize (Zea mays L.) DNA sequences homologous to the oncogenes myb, ras, and src, Genome, 30, 820, 1988.
162. Matsui, M., Sasamoto, S., Kunieda, T., Nomura, N., and Ishizaki, R., Cloning of ara, a putative Arabidopsis thaliana gene homologous to thw ras-related gene family, Gene, 76, 313, 1989.
163. 1+-dependent swelling of etiolated wheat protoplasts, Physiol. Plant., 80, 55, 1990.
164. Anuntalabhochai, S., Terryn, N., Van Montagu, M., and Inzé, D., Molecular characterization of an Arabidopsis thaliana cDNA encoding a small GTP-binding protein, Rha 1, Plant J., 1, 167, 1991.
165. + channel current in guard cells of fava bean, Plant Cell, 3, 1037, 1991.
166. Dallmann, G., Sticher, L., Marshallsay, C., and Nagy, F., Molecular characterization of tobacco cDNAs encoding two small GTP-binding proteins, Plant Mol. Biol., 19, 847, 1992.
167. Hagège, B., Andeol, Y., Boccara, M., Schmitt, P., Jeltsch, J.-M., Barrientos, E., Signoret, J., and Gaspar, T., Ras-related proto-oncogenes are transcripted in leaves and callus from sugarbeet, J. Plant Physiol., 139, 509, 1992.
168. Palme, K., Diefenthal, T., Vingron, M., Sander, C., and Schell, J., Molecular cloning and structural analysis of genes from Zea mays (L.) coding for members of the ras-related ypt gene family, Proc. Natl. Acad. Sci. U.S.A., 89, 787, 1992.
169. Drew, J. E., Bown, D., and Gatehouse, J. A., Sequence of a novel plant ras-related cDNA from Pisum sativum, Plant Mol. Biol., 21, 1195, 1993.
170. Terryn, N., Van Montagu, M., and Inzé, D., GTP-binding proteins in plants, Plant Mol. Biol., 22, 143, 1993.
171. Terryn, N., Arias, M. B., Engler, G., Tiré, C., Villarroel, R., Van Montagu, M., and Inzé, D., rha 1, a gene encoding a small GTP binding protein from Arabidopsis, is expressed primarily in developing guard cells, Plant Cell, 5, 1761, 1993.
172. Yang, Z. and Watson, J. C., Molecular cloning and characterization of rho, a ras-related small GTP-binding protein from the garden pea, Proc. Natl. Acad. Sci. U.S.A., 90, 8732, 1993.
173. Bednarek, S. Y., Reynolds, T. L., Schroeder, M., Grabowski, R., Hengst, L., Gallwitz, D., and Raikhel, N. V., A small GTP-binding protein from Arabidopsis thaliana functionally complements the yeast YPT6 null mutant, Plant Physiol., 104, 591, 1994.
174. Borg, S. and Poulsen, C., Molecular analysis of two Ypt/Rab-related sequences isolated from soybean (Glycine max) DNA libraries, Plant Mol. Biol., 26, 175, 1994.
175. Bowler, C., Neuhaus, G., Yamagata, H., and Chua, N.-H., Cyclic GMP and calcium mediate phytochrome phototransduction, Cell, 77, 73, 1994.
176. Verma, D. P. S., Cheon, C.-I., and Hong, Z., Small GTP-binding proteins and membrane biogenesis in plants, Plant Physiol., 106, 1, 1994.
177. Frederick, S. E., Mangan, M. E., Carey, J. B., and Gruber, P. J., Intermediate filament antigens of 60 and 65 kDa in the nuclear matrix of plants: Their detection and localization, Exp. Cell Res., 199, 213, 1992.
178. McNulty, A. K. and Saunders, M. J., Purification and immunological detection of pea nuclear intermediate filaments: Evidence for plant nuclear lamins, J. Cell Sci., 103, 407, 1992.
179. Li, H. and Roux, S. J., Casein kinase II protein kinase is bound to lamina-matrix and phosphorylates lamin-like protein in isolated pea nuclei, Proc. Natl. Acad. Sci. U.S.A., 89, 8434, 1992.
180. Tong, C.-G., Dauwalder, M., Clawson, G. A., Hatem, C. L., aud Roux, S. J., The major nucleoside triphosphatase in pea (Pisum sativum L.) nuclei and in rat liver nuclei share common epitopes also present in nuclear lamins, Plant Physiol., 101, 1005, 1993.
181. Blumenthal, S. S. D. and Roux, S. J., Immunological analyses of lamin-like proteins in pea nuclei, Suppl. Plant Physiol., 105, 58, 1994.
182. Hsieh, H.-L. and Roux, S. J., Cloning and expression of a gene encoding a nuclear-envelope associated calmodulin-regulated nucleoside triphosphatase, Suppl. Plant Physiol., 105, 75, 1994.
183. Biermann, B. J., Morehead, T. A., Tate, S. E., Price, J. R., Randall, S. K., and Crowell, D. N., Novel isoprenylated proteins identified by an expression library screen, J. Biol. Chem., 269, 25251, 1994.
184. Tate, S. E., Crowell, D. N., and Randall, S. K., Unpublished observations.
185. Morehead, T. A., Biermann, B. J., Crowell, D. N., and Randall, S. K., Changes in protein isoprenylation during the growth of suspension-cultured tobacco cells, Plant Physiol., 109, 277, 1995.
186. Parmryd, I., Shipton, C. A., Swiezewska, E., Andersson, B., and Dallner, G., Identification of spinach farnesyl protein transferase: Dithiothreitol as an acceptor in vitro, Eur. J. Biochem., 234, 723, 1996.
187. Loraine, A. E., Yalovsky, S., Fabry, S., and Gruissem, W., Tomato Rab1A homologs as molecular tools for studying Rab geranylgeranyl transferase in plant cells, Plant Physiol., 110, 1337, 1996.
188. Yaluvsky, S., Loraine, A. E., and Gruissem, W., Specific prenylation of tomato Rab proteins by geranylgeranyl type-II transferase requires a conserved cysteine-cysteine motif, Plant Physiol., 110, 1349, 1996.
189. Biermann, B., Randall, S. K., and Crowell, D. N., Identification and isoprenylation of plant GTP-binding proteins, Plant Mol. Biol., in press.
190. Lin, Y, Wang, Y., Zhu, J.-K, and Yang, Z., Localization of a Rho GTPase implies a role in tip growth and movement of the generative cell in pollen tubes, Plant Cell, 8, 293, 1996.
191. Delmer, D. P., Pear, J. R., Andrawis, A., and Stalker, D. M., Genes encoding small GTP-binding proteins analogous to mammalian rac are preferentially expressed in developing cotton fibers, Mol. Gen. Genet., 248, 43, 1995.
192. Crowell, D. N., Biermann, B. J., and Randall, S. K., Identification of cDNAs encoding isoprenylated proteins, Mol. Biotech., 5, 253, 1996.