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Volumn 1, Issue 5, 2015, Pages

A rubber transferase activator is necessary for natural rubber biosynthesis in dandelion

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EID: 85137325099     PISSN: None     EISSN: 20550278     Source Type: Journal    
DOI: 10.1038/NPLANTS.2015.48     Document Type: Article
Times cited : (78)

References (46)
  • 1
    • 0035051051 scopus 로고    scopus 로고
    • Biochemistry of natural rubber, a vital raw material, emphasizing biosynthetic rate, molecular weight and compartmentalization, in evolutionarily divergent plant species
    • Cornish, K. Biochemistry of natural rubber, a vital raw material, emphasizing biosynthetic rate, molecular weight and compartmentalization, in evolutionarily divergent plant species. Nature Prod. Rep.18, 182–189 (2001).
    • (2001) Nature Prod. Rep. , vol.18 , pp. 182-189
    • Cornish, K.1
  • 2
    • 0002826252 scopus 로고    scopus 로고
    • The rubber industry’s biological nightmare
    • Davis, W. The rubber industry’s biological nightmare. Fortune 136, 86 (1997).
    • (1997) Fortune , vol.136 , pp. 86
    • Davis, W.1
  • 4
    • 38949111519 scopus 로고    scopus 로고
    • Guayule and Russian dandelion as alternative sources of natural rubber
    • van Beilen, J. B. & Poirier, Y. Guayule and Russian dandelion as alternative sources of natural rubber. Crit. Rev. Biotechnol. 27, 217–231 (2007).
    • (2007) Crit. Rev. Biotechnol. , vol.27 , pp. 217-231
    • van Beilen, J.B.1    Poirier, Y.2
  • 5
    • 0000976688 scopus 로고
    • The biosynthesis of rubber. Incorporation of mevalonate and isopentenyl pyrophosphate into rubber by Hevea brasiliensis-latex fractions
    • Archer, B., Audley, B., Cockbain, E. & McSweeney, G. The biosynthesis of rubber. Incorporation of mevalonate and isopentenyl pyrophosphate into rubber by Hevea brasiliensis-latex fractions. Biochem. J. 89, 565 (1963).
    • (1963) Biochem. J. , vol.89 , pp. 565
    • Archer, B.1    Audley, B.2    Cockbain, E.3    McSweeney, G.4
  • 6
    • 11544324496 scopus 로고    scopus 로고
    • Enzymatic aspects of isoprenoid chain elongation
    • Ogura, K. & Koyama, T. Enzymatic aspects of isoprenoid chain elongation. Chem. Rev. 98, 1263–1276 (1998).
    • (1998) Chem. Rev. , vol.98 , pp. 1263-1276
    • Ogura, K.1    Koyama, T.2
  • 7
    • 84857946109 scopus 로고    scopus 로고
    • Laticifer-specific cis-prenyltransferase silencing affects the rubber, triterpene, and inulin content of Taraxacum brevicorniculatum
    • Post, J. et al. Laticifer-specific cis-prenyltransferase silencing affects the rubber, triterpene, and inulin content of Taraxacum brevicorniculatum. Plant Physiol. 158, 1406–1417 (2012).
    • (2012) Plant Physiol , vol.158 , pp. 1406-1417
    • Post, J.1
  • 8
    • 77649279177 scopus 로고    scopus 로고
    • Characterization of rubber particles and rubber chain elongation in Taraxacum koksaghyz
    • Schmidt, T. et al. Characterization of rubber particles and rubber chain elongation in Taraxacum koksaghyz. BMC Biochem 11, 11 (2010).
    • (2010) BMC Biochem , vol.11 , pp. 11
    • Schmidt, T.1
  • 9
    • 0345256451 scopus 로고    scopus 로고
    • Molecular cloning, expression and characterization of cDNA encoding cis-prenyltransferases from Hevea brasiliensis
    • Asawatreratanakul, K. et al. Molecular cloning, expression and characterization of cDNA encoding cis-prenyltransferases from Hevea brasiliensis. Eur. J. Biochem. 270, 4671–4680 (2003).
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4671-4680
    • Asawatreratanakul, K.1
  • 10
    • 84862017434 scopus 로고    scopus 로고
    • Altered levels of the Taraxacum kok-saghyz (Russian dandelion) small rubber particle protein, TkSRPP3, result in qualitative and quantitative changes in rubber metabolism
    • Collins-Silva, J. et al. Altered levels of the Taraxacum kok-saghyz (Russian dandelion) small rubber particle protein, TkSRPP3, result in qualitative and quantitative changes in rubber metabolism. Phytochemistry 79, 46–56 (2012).
    • (2012) Phytochemistry , vol.79 , pp. 46-56
    • Collins-Silva, J.1
  • 11
    • 84864229932 scopus 로고    scopus 로고
    • Down-regulation of small rubber particle protein expression affects integrity of rubber particles and rubber content in Taraxacum brevicorniculatum
    • Hillebrand, A. et al. Down-regulation of small rubber particle protein expression affects integrity of rubber particles and rubber content in Taraxacum brevicorniculatum. PloS ONE 7, e41874 (2012).
    • (2012) Plos ONE , vol.7
    • Hillebrand, A.1
  • 12
    • 0037322820 scopus 로고    scopus 로고
    • Molecular analysis of cis-prenyl chain elongating enzymes
    • Kharel, Y. & Koyama, T. Molecular analysis of cis-prenyl chain elongating enzymes. Nature Prod. Rep. 20, 111–118 (2003).
    • (2003) Nature Prod. Rep. , vol.20 , pp. 111-118
    • Kharel, Y.1    Koyama, T.2
  • 13
    • 33644934032 scopus 로고    scopus 로고
    • Manipulation of prenyl chain length determination mechanism of cis-prenyltransferases
    • Kharel, Y., Takahashi, S., Yamashita, S. & Koyama, T. Manipulation of prenyl chain length determination mechanism of cis-prenyltransferases. FEBS J. 273, 647–657 (2006).
    • (2006) FEBS J , vol.273 , pp. 647-657
    • Kharel, Y.1    Takahashi, S.2    Yamashita, S.3    Koyama, T.4
  • 14
    • 41349104685 scopus 로고    scopus 로고
    • Polyisoprenoid alcohols— recent results of structural studies
    • Skorupinska-Tudek, K., Wojcik, J. & Swiezewska, E. Polyisoprenoid alcohols— recent results of structural studies. Chem. Record 8, 33–45 (2008).
    • (2008) Chem. Record , vol.8 , pp. 33-45
    • Skorupinska-Tudek, K.1    Wojcik, J.2    Swiezewska, E.3
  • 15
    • 33748564953 scopus 로고    scopus 로고
    • Structure and function of cis-prenyl chain elongating enzymes
    • Takahashi, S. & Koyama, T. Structure and function of cis-prenyl chain elongating enzymes. Chem. Record 6, 194–205 (2006).
    • (2006) Chem. Record , vol.6 , pp. 194-205
    • Takahashi, S.1    Koyama, T.2
  • 16
    • 0034698361 scopus 로고    scopus 로고
    • Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis
    • Cunillera, N., Arró, M., Forés, O., Manzano, D. & Ferrer, A. Characterization of dehydrodolichyl diphosphate synthase of Arabidopsis thaliana, a key enzyme in dolichol biosynthesis. FEBS Lett. 477, 170–174 (2000).
    • (2000) FEBS Lett , vol.477 , pp. 170-174
    • Cunillera, N.1    Arró, M.2    Forés, O.3    Manzano, D.4    Ferrer, A.5
  • 17
    • 0037456053 scopus 로고    scopus 로고
    • Identification of human dehydrodolichyl diphosphate synthase gene
    • Endo, S., Zhang, Y.-W., Takahashi, S. & Koyama, T. Identification of human dehydrodolichyl diphosphate synthase gene. Biochim. Biophys. Acta 1625, 291–295 (2003).
    • (2003) Biochim. Biophys. Acta , vol.1625 , pp. 291-295
    • Endo, S.1    Zhang, Y.-W.2    Takahashi, S.3    Koyama, T.4
  • 18
    • 0034945070 scopus 로고    scopus 로고
    • Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis
    • Sato, M., Fujisaki, S., Sato, K., Nishimura, Y. & Nakano, A. Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis. Genes Cells 6, 495–506 (2001).
    • (2001) Genes Cells , vol.6 , pp. 495-506
    • Sato, M.1    Fujisaki, S.2    Sato, K.3    Nishimura, Y.4    Nakano, A.5
  • 19
    • 0032909653 scopus 로고    scopus 로고
    • The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis
    • Sato, M. et al. The yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesis. Mol. Cell. Biol. 19, 471–483 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 471-483
    • Sato, M.1
  • 20
    • 0034743158 scopus 로고    scopus 로고
    • The ins(ide) and outs(ide) of dolichyl phosphate biosynthesis and recycling in the endoplasmic reticulum
    • Schenk, B., Fernandez, F. & Waechter, C. J. The ins(ide) and outs(ide) of dolichyl phosphate biosynthesis and recycling in the endoplasmic reticulum. Glycobiology 11, 61R–70R (2001).
    • (2001) Glycobiology , vol.11 , pp. 61R-70R
    • Schenk, B.1    Fernandez, F.2    Waechter, C.J.3
  • 21
    • 84874243665 scopus 로고    scopus 로고
    • The tomato cis-prenyltransferase gene family
    • Akhtar, T. A. et al. The tomato cis-prenyltransferase gene family. Plant J. 73, 640–652 (2013).
    • (2013) Plant J , vol.73 , pp. 640-652
    • Akhtar, T.A.1
  • 22
    • 84867100495 scopus 로고    scopus 로고
    • Identification and characterization of a cis, trans-mixed heptaprenyl diphosphate synthase from Arabidopsis thaliana
    • Kera, K., Takahashi, S., Sutoh, T., Koyama, T. & Nakayama, T. Identification and characterization of a cis, trans-mixed heptaprenyl diphosphate synthase from Arabidopsis thaliana. FEBS J. 279, 3813–3827 (2012).
    • (2012) FEBS J , vol.279 , pp. 3813-3827
    • Kera, K.1    Takahashi, S.2    Sutoh, T.3    Koyama, T.4    Nakayama, T.5
  • 23
    • 84891134385 scopus 로고    scopus 로고
    • cis-Prenyltransferase AtCPT6 produces a family of very short-chain polyisoprenoids in planta
    • Surmacz, L., Plochocka, D., Kania, M., Danikiewicz, W. & Swiezewska, E. cis-Prenyltransferase AtCPT6 produces a family of very short-chain polyisoprenoids in planta. Biochim. Biophys. 1841, 240–250 (2014).
    • (2014) Biochim. Biophys. , vol.1841 , pp. 240-250
    • Surmacz, L.1    Plochocka, D.2    Kania, M.3    Danikiewicz, W.4    Swiezewska, E.5
  • 24
    • 79958803662 scopus 로고    scopus 로고
    • Nogo-B receptor is necessary for cellular dolichol biosynthesis and protein N-glycosylation
    • Harrison, K. D. et al. Nogo-B receptor is necessary for cellular dolichol biosynthesis and protein N-glycosylation. EMBO J. 30, 2490–2500 (2011).
    • (2011) EMBO J , vol.30 , pp. 2490-2500
    • Harrison, K.D.1
  • 25
    • 0035836712 scopus 로고    scopus 로고
    • Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase
    • Fujihashi, M. et al. Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase. Proc. Natl Acad. Sci. USA 98, 4337–4342 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 4337-4342
    • Fujihashi, M.1
  • 26
    • 69149089283 scopus 로고    scopus 로고
    • Nogo-B receptor stabilizes Niemann-Pick type C2 protein and regulates intracellular cholesterol trafficking
    • Harrison, K. D. et al. Nogo-B receptor stabilizes Niemann-Pick type C2 protein and regulates intracellular cholesterol trafficking. Cell Metab. 10, 208–218 (2009).
    • (2009) Cell Metab , vol.10 , pp. 208-218
    • Harrison, K.D.1
  • 27
    • 33746622474 scopus 로고    scopus 로고
    • Identification of a receptor necessary for Nogo-B stimulated chemotaxis and morphogenesis of endothelial cells
    • Miao, R. Q. et al. Identification of a receptor necessary for Nogo-B stimulated chemotaxis and morphogenesis of endothelial cells. Proc. Natl Acad. Sci. USA 103, 10997–11002 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 10997-11002
    • Miao, R.Q.1
  • 28
    • 0035832806 scopus 로고    scopus 로고
    • Similarities and differences in rubber biochemistry among plant species
    • Cornish, K. Similarities and differences in rubber biochemistry among plant species. Phytochemistry 57, 1123–1134 (2001).
    • (2001) Phytochemistry , vol.57 , pp. 1123-1134
    • Cornish, K.1
  • 29
    • 33646168160 scopus 로고    scopus 로고
    • Lipid droplets: A unified view of a dynamic organelle
    • Martin, S. & Parton, R. G. Lipid droplets: a unified view of a dynamic organelle. Nature Rev. Mol. Cell Biol. 7, 373–378 (2006).
    • (2006) Nature Rev. Mol. Cell Biol. , vol.7 , pp. 373-378
    • Martin, S.1    Parton, R.G.2
  • 30
    • 77952876943 scopus 로고    scopus 로고
    • Molecular cloning and characterization of rubber biosynthetic genes from Taraxacum koksaghyz
    • Schmidt, T. et al. Molecular cloning and characterization of rubber biosynthetic genes from Taraxacum koksaghyz. Plant Mol. Biol. Report. 28, 277–284 (2010).
    • (2010) Plant Mol. Biol. Report. , vol.28 , pp. 277-284
    • Schmidt, T.1
  • 32
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: Discriminating signal peptides from transmembrane regions
    • Petersen, T. N., Brunak, S., von Heijne, G. & Nielsen, H. SignalP 4.0: discriminating signal peptides from transmembrane regions. Nature Methods 8, 785–786 (2011).
    • (2011) Nature Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 33
    • 0000207681 scopus 로고
    • TMbase-A database of membrane spanning protein segments
    • Hofmann, K. TMbase-A database of membrane spanning protein segments. Biol. Chem. Hoppe-Seyler 374, 166 (1993).
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1
  • 34
    • 57749115921 scopus 로고    scopus 로고
    • Dolichol biosynthesis and its effects on the unfolded protein response and abiotic stress resistance in Arabidopsis
    • Zhang, H. et al. Dolichol biosynthesis and its effects on the unfolded protein response and abiotic stress resistance in Arabidopsis. Plant Cell Online 20, 1879–1898 (2008).
    • (2008) Plant Cell Online , vol.20 , pp. 1879-1898
    • Zhang, H.1
  • 35
    • 84860216728 scopus 로고    scopus 로고
    • A novel method for monitoring the localization of cytochromes P450 and other endoplasmic reticulum membrane associated proteins: A tool for investigating the formation of metabolons
    • Bassard, J. E., Mutterer, J., Duval, F. & Werck-Reichhart, D. A novel method for monitoring the localization of cytochromes P450 and other endoplasmic reticulum membrane associated proteins: a tool for investigating the formation of metabolons. FEBS J. 279, 1576–1583 (2012).
    • (2012) FEBS J , vol.279 , pp. 1576-1583
    • Bassard, J.E.1    Mutterer, J.2    Duval, F.3    Werck-Reichhart, D.4
  • 36
    • 84913596346 scopus 로고    scopus 로고
    • Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation
    • Park, E. J. et al. Mutation of Nogo-B receptor, a subunit of cis-prenyltransferase, causes a congenital disorder of glycosylation. Cell Metab. 20, 448–457 (2014).
    • (2014) Cell Metab , vol.20 , pp. 448-457
    • Park, E.J.1
  • 37
    • 77956518051 scopus 로고    scopus 로고
    • Molecular characterization of the cis-prenyltransferase of Giardia lamblia
    • Grabińska, K. A. et al. Molecular characterization of the cis-prenyltransferase of Giardia lamblia. Glycobiology 20, 824–832 (2010).
    • (2010) Glycobiology , vol.20 , pp. 824-832
    • Grabińska, K.A.1
  • 38
    • 84904039647 scopus 로고    scopus 로고
    • ATP citrate lyase activity is post-translationally regulated by sink strength and impacts the wax, cutin and rubber biosynthetic pathways
    • Xing, S. et al. ATP citrate lyase activity is post-translationally regulated by sink strength and impacts the wax, cutin and rubber biosynthetic pathways. Plant J. (2014).
    • (2014) Plant J
    • Xing, S.1
  • 39
    • 84860331610 scopus 로고    scopus 로고
    • Proteomic analysis of latex from the rubber-producing plant Taraxacum brevicorniculatum
    • Wahler, D. et al. Proteomic analysis of latex from the rubber-producing plant Taraxacum brevicorniculatum. Proteomics 12, 901–905 (2012).
    • (2012) Proteomics , vol.12 , pp. 901-905
    • Wahler, D.1
  • 40
    • 0033406808 scopus 로고    scopus 로고
    • Rubber particles from four different species, examined by transmission electron microscopy and electron-paramagnetic-resonance spin labeling, are found to consist of a homogeneous rubber core enclosed by a contiguous, monolayer biomembrane
    • Cornish, K., Wood, D. F. & Windle, J. J. Rubber particles from four different species, examined by transmission electron microscopy and electron-paramagnetic-resonance spin labeling, are found to consist of a homogeneous rubber core enclosed by a contiguous, monolayer biomembrane. Planta 210, 85–96 (1999).
    • (1999) Planta , vol.210 , pp. 85-96
    • Cornish, K.1    Wood, D.F.2    Windle, J.J.3
  • 41
    • 0026545550 scopus 로고
    • Surface structure and properties of plant seed oil bodies
    • Tzen, J. & Huang, A. Surface structure and properties of plant seed oil bodies. J. Cell Biol. 117, 327–335 (1992).
    • (1992) J. Cell Biol. , vol.117 , pp. 327-335
    • Tzen, J.1    Huang, A.2
  • 42
    • 84855708946 scopus 로고    scopus 로고
    • Biogenesis and functions of lipid droplets in plants. Thematic Review Series: Lipid droplet synthesis and metabolism: From yeast to man
    • Chapman, K. D., Dyer, J. M. & Mullen, R. T. Biogenesis and functions of lipid droplets in plants. Thematic Review Series: lipid droplet synthesis and metabolism: from yeast to man. J. Lipid Res. 53, 215–226 (2012).
    • (2012) J. Lipid Res. , vol.53 , pp. 215-226
    • Chapman, K.D.1    Dyer, J.M.2    Mullen, R.T.3
  • 43
    • 84922106694 scopus 로고    scopus 로고
    • A lettuce (Lactuca sativa) homolog of human Nogo-B receptor interacts with cis-prenyltransferase and is necessary for natural rubber biosynthesis
    • Qu, Y. et al. A lettuce (Lactuca sativa) homolog of human Nogo-B receptor interacts with cis-prenyltransferase and is necessary for natural rubber biosynthesis. J. Biol. Chem. 290, 1898–1914 (2015).
    • (2015) J. Biol. Chem. , vol.290 , pp. 1898-1914
    • Qu, Y.1
  • 44
    • 78149357953 scopus 로고    scopus 로고
    • Recombinant artificial forisomes provide ample quantities of smart biomaterials for use in technical devices
    • Müller, B. et al. Recombinant artificial forisomes provide ample quantities of smart biomaterials for use in technical devices. Appl. Microbiol. Biotechnol. 88, 689–698 (2010).
    • (2010) Appl. Microbiol. Biotechnol. , vol.88 , pp. 689-698
    • Müller, B.1
  • 45
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. & Gordon, J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl Acad. Sci. USA 76, 4350–4354 (1979).
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 46
    • 0024799254 scopus 로고
    • High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier
    • Schiestl, R. H. & Gietz, R. D. High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr. Genet. 16, 339–346 (1989).
    • (1989) Curr. Genet. , vol.16 , pp. 339-346
    • Schiestl, R.H.1    Gietz, R.D.2


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