SEARCH

SEARCH BY CITATION

References

  • Ambo, T., Noike, M., Kurokawa, H. and Koyama, T. (2008) Cloning and functional analysis of novel short-chain cis–prenyltransferases. Biochem. Biophys. Res. Commun. 375, 536540.
  • Asawatreratanakul, K., Zhang, Y.W., Wititsuwannakul, D., Wititsuwannakul, R., Takahashi, S., Rattanapittayaporn, A. and Koyama, T. (2003) Molecular cloning, expression and characterization of cDNA encoding cis–prenyltransferases from Hevea brasiliensis. A key factor participating in natural rubber biosynthesis. Eur. J. Biochem. 270, 46714680.
  • Austin, J.R. II, Frost, E., Vidi, P.A., Kessler, F. and Staehelin, L.A. (2006) Plastoglobules are lipoprotein subcompartments of the chloroplast that are permanently coupled to thylakoid membranes and contain biosynthetic enzymes. Plant Cell, 18, 16931703.
  • Bajda, A., Chojnacki, T., Hertel, J., Swiezewska, E., Wojcik, J., Kaczkowska, A., Marczewski, A., Bojarczuk, T., Karolewski, P. and Oleksyn, J. (2005) Light conditions alter accumulation of long chain polyprenols in leaves of trees and shrubs throughout the vegetation season. Acta Biochim. Pol. 52, 233241.
  • Bonk, M., Hoffmann, B., Von Lintig, J., Schledz, M., Al–Babili, S., Hobeika, E., Kleinig, H. and Beyer, P. (1997) Chloroplast import of four carotenoid biosynthetic enzymes in vitro reveals differential fates prior to membrane binding and oligomeric assembly. Eur. J. Biochem. 247, 942950.
  • Burke, C.C., Wildung, M.R. and Croteau, R. (1999) Geranyl diphosphate synthase: cloning, expression, and characterization of this prenyltransferase as a heterodimer. Proc. Natl Acad. Sci. USA, 96, 1306213067.
  • Cheniclet, C., Rafia, F., Saint-Guily, A., Verna, A. and Carde, J.P. (1992) Localization of the enzyme geranylgeranylpyrophosphate synthase in Capsicum fruits by immunogold cytochemistry after conventional chemical fixation or quick-freezing by freeze-substitution. Labelling evolution during fruit ripening. Biol. Cell, 75, 145154.
  • Chojnacki, T. and Vogtman, T. (1984) The occurrence and seasonal distribution of C50–C60 polyprenols and of C100 and similar long-chain polyprenols in leaves of plants. Acta Biochim. Pol. 31, 115126.
  • Ciepichal, E., Jemiola-Rzeminska, M., Hertel, J., Swiezewska, E. and Strzalka, K. (2011) Configuration of polyisoprenoids affects the permeability and thermotropic properties of phospholipid/polyisoprenoid model membranes. Chem. Phys. Lipids 164, 300306.
  • Cunillera, N., Arró, M., Forés, O., Manzano, D. and Ferrer, A. (2000) Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis. FEBS Lett. 477, 170174.
  • van Der Hoeven, R.S., Monforte, A.J., Breeden, D., Tanksley, S.D. and Steffens, J.C. (2000) Genetic control and evolution of sesquiterpene biosynthesis in Lycopersicon esculentum and L. hirsutum. Plant Cell, 12, 22832294.
  • Ducluzeau, A.L., Wamboldt, Y., Elowsky, C.G., Mackenzie, S.A., Schuurink, R.C. and Basset, G.J. (2012) Gene network reconstruction identifies the authentic trans–prenyl diphosphate synthase that makes the solanesyl moiety of ubiquinone–9 in Arabidopsis. Plant J. 69, 366375.
  • Eugeni-Piller, L., Besagni, C., Ksas, B., Rumeau, D., Bréhélin, C., Glauser, G., Kessler, F. and Havaux, M. (2011) Chloroplast lipid droplet type II NAD(P)H quinone oxidoreductase is essential for prenylquinone metabolism and vitamin K1 accumulation. Proc. Natl Acad. Sci. USA, 108, 1435414359.
  • Falara, V., Akhtar, T.A., Nguyen, T.T.H. et al. (2011) The tomato terpene synthase gene family. Plant Physiol. 157, 770789.
  • Foster, T.M., Lough, T.J., Emerson, S.J., Lee, R.H., Bowman, J.L., Forster, R.L. and Lucas, W.J. (2002) A surveillance system regulates selective entry of RNA into the shoot apex. Plant Cell, 14, 14971508.
  • Fridman, E., Wang, J., Iijima, Y., Froehlich, J.E., Gang, D.R., Ohlrogge, J. and Pichersky, E. (2005) Metabolic, genomic, and biochemical analyses of glandular trichomes from the wild tomato species Lycopersicon hirsutum identify a key enzyme in the biosynthesis of methylketones. Plant Cell, 17, 12521267.
  • Fujihashi, M., Zhang, Y.W., Higuchi, Y., Li, X.Y., Koyama, T. and Miki, K. (2001) Crystal structure of cis–prenyl chain elongating enzyme, undecaprenyl diphosphate synthase. Proc. Natl Acad. Sci. USA, 98, 43374342.
  • Gietz, R.D. and Schiestl, R.H. (2007) Large-scale high-efficiency yeast transformation using the LiAc/SS carrier DNA/PEG method. Nat. Protoc. 2, 3841.
  • Hajdukiewicz, P., Svab, Z. and Maliga, P. (1994) The small, versatile pPZP family of Agrobacterium binary vectors for plant transformation. Plant Mol. Biol. 25, 989994.
  • Harrison, K.D., Park, E.J., Gao, N., Kuo, A., Rush, J.S., Waechter, C.J., Lehrman, M.A. and Sessa, W.C. (2011) Nogo–B receptor is necessary for cellular dolichol biosynthesis and protein N–glycosylation. EMBO J. 30, 24902500.
  • Hirooka, Y., Bamba, T., Fukusaki, E. and Kobayashi, A. (2003) Cloning and kinetic characterization of Arabidopsis thaliana solanesyl diphosphate synthase. Biochem. J. 370, 679686.
  • Kera, K., Takahashi, S., Sutoh, T., Koyama, T. and Nakayama, T. (2012) Identification and characterization of a cis,trans–mixed heptaprenyl diphosphate synthase from Arabidopsis thaliana. FEBS J. 279, 38133827.
  • Kharel, Y. and Koyama, T. (2003) Molecular analysis of cis–prenyl chain elongating enzymes. Nat. Prod. Rep. 20, 111118.
  • Kharel, Y., Takahashi, S., Yamashita, S. and Koyama, T. (2006) Manipulation of prenyl chain length determination mechanism of cis-prenyltransferases. FEBS J. 273, 647657.
  • Kirby, J. and Keasling, J.D. (2009) Biosynthesis of plant isoprenoids: perspectives for microbial engineering. Annu. Rev. Plant Biol. 60, 335355.
  • Lange, B.M. and Ghassemian, M. (2003) Genome organization in Arabidopsis thaliana: a survey for genes involved in isoprenoid and chlorophyll metabolism. Plant Mol. Biol. 51, 925948.
  • Liang, P.H., Ko, T.P. and Wang, A.H. (2002) Structure, mechanism, and function of prenyltransferases. Eur. J. Biochem. 269, 33393354.
  • Liu, M.C., Wang, B.J., Huang, J.K. and Wang, C.S. (2011) Expression, localization and function of a cis–prenyltransferase in the tapetum and microspores of lily anthers. Plant Cell Physiol. 52, 14871500.
  • McGarvey, D.J. and Croteau, R. (1995) Terpenoid metabolism. Plant Cell 7, 10151026.
  • Nelson, B.K., Cai, X. and Nebenführ, A. (2007) A multicolored set of in vivo organelle markers for co-localization studies in Arabidopsis and other plants. Plant J. 51, 11261136.
  • Oh, S.K., Han, K.H., Ryu, S.B. and Kang, H. (2000) Molecular cloning, expression, and functional analysis of a cis–prenyltransferase from Arabidopsis thaliana: implications in rubber biosynthesis. J. Biol. Chem. 275, 1848218488.
  • Phillips, M.A., D'Auria, J.C., Gershenzon, J. and Pichersky, E. (2008) The Arabidopsis thaliana type I isopentenyl diphosphate isomerases are targeted to multiple subcellular compartments and have overlapping functions in isoprenoid biosynthesis. Plant Cell 20, 677696.
  • Post, J., van Deenen, N., Fricke, J. et al. (2012) Laticifer-specific cis–prenyltransferase silencing affects the rubber, triterpene, and inulin content of Taraxacum brevicorniculatum. Plant Physiol. 158, 14061417.
  • Rodríguez-Concepción, M. and Boronat, A. (2002) Elucidation of the methylerythritol phosphate pathway for isoprenoid biosynthesis in bacteria and plastids. A metabolic milestone achieved through genomics. Plant Physiol. 130, 10791089.
  • Rush, J.S., Matveev, S., Guan, Z., Raetz, C.R.H. and Waechter, C.J. (2010) Expression of functional bacterial undecaprenyl pyrophosphate synthase in the yeast rer2∆ mutant and CHO cells. Glycobiology, 20, 15851593.
  • Sakaihara, T., Honda, A., Tateyama, S. and Sagami, H. (2000) Subcellular fractionation of polyprenyl diphosphate synthase activities responsible for the syntheses of polyprenols and dolichols in spinach leaves. J. Biochem. 128, 10731078.
  • Sallaud, C., Rontein, D., Onillon, S. et al. (2009) A novel pathway for sesquiterpene biosynthesis from Z,Z–farnesyl pyrophosphate in the wild tomato Solanum habrochaites. Plant Cell 21, 301317.
  • Sanmiya, K., Ueno, O., Matsuoka, M. and Yamamoto, N. (1999) Localization of farnesyl diphosphate synthase in chloroplasts. Plant Cell Physiol. 40, 348354.
  • Sato, M., Sato, K., Nishikawa, S., Hirata, A., Kato, J. and Nakano, A. (1999) The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis–prenyltransferase, a key enzyme in dolichol synthesis. Mol. Cell. Biol. 19, 471483.
  • Schenk, B., Fernandez, F. and Waechter, C.J. (2001) The inside and outside of dolichyl phosphate biosynthesis and recycling in the endoplasmic reticulum. Glycobiology 11, 6170.
  • Schilmiller, A.L., Schauvinhold, I., Larson, M., Xu, R., Charbonneau, A.L., Schmidt, A., Wilkerson, C., Last, R.L. and Pichersky, E. (2009) Monoterpenes in the glandular trichomes of tomato are synthesized from a neryl diphosphate precursor rather than geranyl diphosphate. Proc. Natl Acad. Sci. USA 106, 1086510870.
  • Schilmiller, A.L., Miner, D.P., Larson, M., McDowell, E., Gang, D.R., Wilkerson, C. and Last, R.L. (2010) Studies of a biochemical factory: tomato trichome deep expressed sequence tag sequencing and proteomics. Plant Physiol. 153, 12121223.
  • Schmidt, T., Lenders, M., Hillebrand, A., van Deenen, N., Munt, O., Reichelt, R., Eisenreich, W., Fischer, R., Prüfer, D. and Gronover, C.S. (2010) Characterization of rubber particles and rubber chain elongation in Taraxacum koksaghyz. BMC Biochem. 11, 11.
  • Schulbach, M.C., Brennan, P.J. and Crick, D.C. (2000) Identification of a short (C15) chain Z–isoprenyl diphosphate synthase and a homologous long (C50) chain isoprenyl diphosphate synthase in Mycobacterium tuberculosis. J. Biol. Chem. 275, 2287622881.
  • Shridas, P., Rush, J.S. and Waechter, C.J. (2003) Identification and characterization of a cDNA encoding a long-chain cis–isoprenyltranferase involved in dolichyl monophosphate biosynthesis in the ER of brain cells. Biochem. Biophys. Res. Commun. 312, 13491356.
  • Skorupinska-Tudek, K., Wojcik, J. and Swiezewska, E. (2008) Polyisoprenoid alcohols – recent results of structural studies. Chem. Rec. 8, 3345.
  • Spurgeon, S.L., Sathyamoorthy, N. and Porter, J.W. (1984) Isopentenyl pyrophosphate isomerase and prenyltransferase from tomato fruit plastids. Arch. Biochem. Biophys. 230, 446454.
  • Surmacz, L. and Swiezewska, E. (2011) Polyisoprenoids – secondary metabolites or physiologically important superlipids? Biochem. Biophys. Res. Commun. 407, 627632.
  • Swiezewska, E. and Danikiewicz, W. (2005) Polyisoprenoids: structure, biosynthesis and function. Prog. Lipid Res. 44, 235258.
  • Swiezewska, E., Sasak, W., Mańkowski, T., Jankowski, W., Vogtman, T., Krajewska, I., Hertel, J., Skoczylas, E. and Chojnacki, T. (1994) The search for plant polyprenols. Acta Biochim. Pol. 41, 221260.
  • Tamura, K., Dudley, J., Nei, M. and Kumar, S. (2007) MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24, 15961599.
  • Tzfira, T., Tian, G.W., Lacroix, B., Vyas, S., Li, J., Leitner-Dagan, Y., Krichevsky, A., Taylor, T., Vainstein, A. and Citovsky, V. (2005) pSAT vectors: a modular series of plasmids for autofluorescent protein tagging and expression of multiple genes in plants. Plant Mol. Biol. 57, 503516.
  • Vigo, C., Grossman, S.H. and Drost-Hansen, W. (1984) Interaction of dolichol and dolichyl phosphate with phospholipid bilayers. Biochim. Biophys. Acta 774, 221226.
  • Vincent, F., Molin, D.D., Weiner, R.M., Bourne, Y. and Henrissat, B. (2010) Structure of a polyisoprenoid binding domain from Saccharophagus degradans implicated in plant cell wall breakdown. FEBS Lett. 584, 15771584.
  • Wu, F.H., Shen, S.C., Lee, L.Y., Lee, S.H., Chan, M.T. and Lin, C.S. (2009) Tape–Arabidopsis sandwich – a simpler Arabidopsis protoplast isolation method. Plant Methods, 5, 16.
  • Ytterberg, A.J., Peltier, J.B. and van Wijk, K.J. (2006) Protein profiling of plastoglobules in chloroplasts and chromoplasts. A surprising site for differential accumulation of metabolic enzymes. Plant Physiol. 140, 984997.
  • Yu, L., Peña-Castillo, L., Mnaimneh, S., Hughes, T.R. and Brown, G.W. (2006) A survey of essential gene function in the yeast cell division cycle. Mol. Biol. Cell 11, 47364747.
  • Yu, G., Nguyen, T.T., Guo, Y., Schauvinhold, I., Auldridge, M.E., Bhuiyan, N., Ben-Israel, I., Iijima, Y., Fridman, E., Noel, J.P. and Pichersky, E. (2010) Enzymatic functions of wild tomato methylketone synthases 1 and 2. Plant Physiol. 154, 6777.
  • Zhang, H., Ohyama, K., Boudet, J., Chen, Z., Yang, J., Zhang, M., Muranaka, T., Maurel, C., Zhu, J.K. and Gong, Z. (2008) Dolichol biosynthesis and its effects on the unfolded protein response and abiotic stress resistance in Arabidopsis. Plant Cell, 20, 18791898.
  • Zhou, G.P. and Troy, F.A. II (2003) Characterization by NMR and molecular modeling of the binding of polyisoprenols and polyisoprenyl recognition sequence peptides: 3D structure of the complexes reveals sites of specific interactions. Glycobiology, 13, 5171.