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Volumn 40, Issue , 2017, Pages 165-175

An endoplasmic reticulum-engineered yeast platform for overproduction of triterpenoids

Author keywords

Combinatorial biosynthesis; Cytochrome P450; Metabolic engineering; Saponins; Terpenoids

Indexed keywords

BIOCHEMISTRY; BIOSYNTHESIS; CELL MEMBRANES; ENZYMES; LIPIDS; METABOLISM; METABOLITES; PHOSPHATASES; PRODUCTION PLATFORMS; YEAST;

EID: 85014353157     PISSN: 10967176     EISSN: 10967184     Source Type: Journal    
DOI: 10.1016/j.ymben.2017.02.007     Document Type: Article
Times cited : (139)

References (55)
  • 1
    • 15544364507 scopus 로고    scopus 로고
    • Genomics-based selection and functional characterization of triterpene glycosyltransferases from the model legume Medicago truncatula
    • Achnine, L., Huhman, D.V., Farag, M.A., Sumner, L.W., Blount, J.W., Dixon, R.A., Genomics-based selection and functional characterization of triterpene glycosyltransferases from the model legume Medicago truncatula. Plant J. 41 (2005), 875–887.
    • (2005) Plant J. , vol.41 , pp. 875-887
    • Achnine, L.1    Huhman, D.V.2    Farag, M.A.3    Sumner, L.W.4    Blount, J.W.5    Dixon, R.A.6
  • 3
    • 35349022993 scopus 로고    scopus 로고
    • ® cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae
    • ® cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae. Yeast 24 (2007), 913–919.
    • (2007) Yeast , vol.24 , pp. 913-919
    • Alberti, S.1    Gitler, A.D.2    Lindquist, S.3
  • 4
    • 70449592325 scopus 로고    scopus 로고
    • Enhancing sesquiterpene production in Saccharomyces cerevisiae through in silico driven metabolic engineering
    • Asadollahi, M.A., Maury, J., Patil, K.R., Schalk, M., Clark, A., Nielsen, J., Enhancing sesquiterpene production in Saccharomyces cerevisiae through in silico driven metabolic engineering. Metab. Eng. 11 (2009), 328–334.
    • (2009) Metab. Eng. , vol.11 , pp. 328-334
    • Asadollahi, M.A.1    Maury, J.2    Patil, K.R.3    Schalk, M.4    Clark, A.5    Nielsen, J.6
  • 7
    • 84951774485 scopus 로고    scopus 로고
    • The UDP-glycosyltransferase (UGT) superfamily expressed in humans, insects and plants: animal–plant arms-race and co-evolution
    • Bock, K.W., The UDP-glycosyltransferase (UGT) superfamily expressed in humans, insects and plants: animal–plant arms-race and co-evolution. Biochem. Pharmacol. 99 (2016), 11–17.
    • (2016) Biochem. Pharmacol. , vol.99 , pp. 11-17
    • Bock, K.W.1
  • 8
    • 79960711299 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum: recent lessons from yeast and mammalian cell systems
    • Brodsky, J.L., Skach, W.R., Protein folding and quality control in the endoplasmic reticulum: recent lessons from yeast and mammalian cell systems. Curr. Opin. Cell Biol. 23 (2011), 464–475.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 464-475
    • Brodsky, J.L.1    Skach, W.R.2
  • 9
    • 79961118496 scopus 로고    scopus 로고
    • Regulation of HMG-CoA reductase in mammals and yeast
    • Burg, J.S., Espenshade, P.J., Regulation of HMG-CoA reductase in mammals and yeast. Prog. Lipid Res. 50 (2011), 403–410.
    • (2011) Prog. Lipid Res. , vol.50 , pp. 403-410
    • Burg, J.S.1    Espenshade, P.J.2
  • 11
    • 23344435534 scopus 로고    scopus 로고
    • Dual activators of the sterol biosynthetic pathway of Saccharomyces cerevisiae: similar activation/regulatory domains but different response mechanisms
    • Davies, B.S.J., Wang, H.S., Rine, J., Dual activators of the sterol biosynthetic pathway of Saccharomyces cerevisiae: similar activation/regulatory domains but different response mechanisms. Mol. Cell. Biol. 25 (2005), 7375–7385.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 7375-7385
    • Davies, B.S.J.1    Wang, H.S.2    Rine, J.3
  • 12
    • 84969508597 scopus 로고    scopus 로고
    • Enhancing antibody folding and secretion by tailoring the Saccharomyces cerevisiae endoplasmic reticulum
    • de Ruijter, J.C., Koskela, E.V., Frey, A.D., Enhancing antibody folding and secretion by tailoring the Saccharomyces cerevisiae endoplasmic reticulum. Microb. Cell Fact., 15, 2016, 87.
    • (2016) Microb. Cell Fact. , vol.15 , pp. 87
    • de Ruijter, J.C.1    Koskela, E.V.2    Frey, A.D.3
  • 13
    • 43149110168 scopus 로고    scopus 로고
    • Identification and characterization of isoflavonoid specific glycosyltransferase and malonyltransferase from soybean seeds
    • Dhaubhadel, S., Farhangkhoee, M., Chapman, R., Identification and characterization of isoflavonoid specific glycosyltransferase and malonyltransferase from soybean seeds. J. Exp. Bot. 59 (2008), 981–994.
    • (2008) J. Exp. Bot. , vol.59 , pp. 981-994
    • Dhaubhadel, S.1    Farhangkhoee, M.2    Chapman, R.3
  • 16
    • 84978680317 scopus 로고    scopus 로고
    • The lipid droplet—a well-connected organelle
    • Gao, Q., Goodman, J.M., The lipid droplet—a well-connected organelle. Front. Cell Dev. Biol., 3, 2015, 49.
    • (2015) Front. Cell Dev. Biol. , vol.3 , pp. 49
    • Gao, Q.1    Goodman, J.M.2
  • 17
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
    • Gietz, R.D., Woods, R.A., Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method. Methods Enzymol. 350 (2002), 87–96.
    • (2002) Methods Enzymol. , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 20
    • 64749083589 scopus 로고    scopus 로고
    • Protein quality control as a strategy for cellular regulation: lessons from ubiquitin-mediated regulation of the sterol pathway
    • Hampton, R.Y., Garza, R.M., Protein quality control as a strategy for cellular regulation: lessons from ubiquitin-mediated regulation of the sterol pathway. Chem. Rev. 109 (2009), 1561–1574.
    • (2009) Chem. Rev. , vol.109 , pp. 1561-1574
    • Hampton, R.Y.1    Garza, R.M.2
  • 21
  • 22
    • 84871384382 scopus 로고    scopus 로고
    • Positive genetic interactors of HMG2 identify a new set of genetic perturbations for improving sesquiterpene production in Saccharomyces cerevisiae
    • Ignea, C., Trikka, F.A., Kourtzelis, I., Argiriou, A., Kanellis, A.K., Kampranis, S.C., Makris, A.M., Positive genetic interactors of HMG2 identify a new set of genetic perturbations for improving sesquiterpene production in Saccharomyces cerevisiae. Microb. Cell Fact., 11, 2012, 162.
    • (2012) Microb. Cell Fact. , vol.11 , pp. 162
    • Ignea, C.1    Trikka, F.A.2    Kourtzelis, I.3    Argiriou, A.4    Kanellis, A.K.5    Kampranis, S.C.6    Makris, A.M.7
  • 23
    • 73649131594 scopus 로고    scopus 로고
    • Plant NADPH-cytochrome P450 oxidoreductases
    • Jensen, K., Møller, B.L., Plant NADPH-cytochrome P450 oxidoreductases. Phytochemistry 71 (2010), 132–141.
    • (2010) Phytochemistry , vol.71 , pp. 132-141
    • Jensen, K.1    Møller, B.L.2
  • 25
    • 41549107616 scopus 로고    scopus 로고
    • Engineering triterpene production in Saccharomyces cerevisiae – β-amyrin synthase from Artemisia annua
    • Kirby, J., Romanini, D.W., Paradise, E.M., Keasling, J.D., Engineering triterpene production in Saccharomyces cerevisiae – β-amyrin synthase from Artemisia annua. FEBS J. 275 (2008), 1852–1859.
    • (2008) FEBS J. , vol.275 , pp. 1852-1859
    • Kirby, J.1    Romanini, D.W.2    Paradise, E.M.3    Keasling, J.D.4
  • 26
    • 0029926584 scopus 로고    scopus 로고
    • Different subcellular localization of Saccharomyces cerevisiae HMG-CoA reductase isozymes at elevated levels corresponds to distinct endoplasmic reticulum membrane proliferations
    • Koning, A.J., Roberts, C.J., Wright, R.L., Different subcellular localization of Saccharomyces cerevisiae HMG-CoA reductase isozymes at elevated levels corresponds to distinct endoplasmic reticulum membrane proliferations. Mol. Biol. Cell. 7 (1996), 769–789.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 769-789
    • Koning, A.J.1    Roberts, C.J.2    Wright, R.L.3
  • 28
    • 0031931498 scopus 로고    scopus 로고
    • Dual localization of squalene epoxidase, Erg1p, in yeast reflects a relationship between the endoplasmic reticulum and lipid particles
    • Leber, R., Landl, K., Zinser, E., Ahorn, H., Spök, A., Kohlwein, S.D., Turnowsky, F., Daum, G., Dual localization of squalene epoxidase, Erg1p, in yeast reflects a relationship between the endoplasmic reticulum and lipid particles. Mol. Biol. Cell. 9 (1998), 375–386.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 375-386
    • Leber, R.1    Landl, K.2    Zinser, E.3    Ahorn, H.4    Spök, A.5    Kohlwein, S.D.6    Turnowsky, F.7    Daum, G.8
  • 29
    • 84938861490 scopus 로고    scopus 로고
    • Nicotinate O-glucosylation is an evolutionarily metabolic trait important for seed germination under stress conditions in Arabidopsis thaliana
    • Li, W., Zhang, F., Chang, Y., Zhao, T., Schranz, M.E., Wang, G., Nicotinate O-glucosylation is an evolutionarily metabolic trait important for seed germination under stress conditions in Arabidopsis thaliana. Plant Cell. 27 (2015), 1907–1924.
    • (2015) Plant Cell. , vol.27 , pp. 1907-1924
    • Li, W.1    Zhang, F.2    Chang, Y.3    Zhao, T.4    Schranz, M.E.5    Wang, G.6
  • 30
    • 84873477374 scopus 로고    scopus 로고
    • Heterologous expression of dammarenediol synthase gene in an engineered Saccharomyces cerevisiae
    • Liang, Y.-L., Zhao, S.-J., Xu, L.-X., Zhang, X.-Y., Heterologous expression of dammarenediol synthase gene in an engineered Saccharomyces cerevisiae. Lett. Appl. Microbiol. 55 (2012), 323–329.
    • (2012) Lett. Appl. Microbiol. , vol.55 , pp. 323-329
    • Liang, Y.-L.1    Zhao, S.-J.2    Xu, L.-X.3    Zhang, X.-Y.4
  • 31
    • 17844376185 scopus 로고    scopus 로고
    • Vacuolar degradation of rat liver CYP2B1 in Saccharomyces cerevisiae: further validation of the yeast model and structural implications for the degradation of mammalian endoplasmic reticulum P450 proteins
    • Liao, M., Zgoda, V.G., Murray, B.P., Correia, M.A., Vacuolar degradation of rat liver CYP2B1 in Saccharomyces cerevisiae: further validation of the yeast model and structural implications for the degradation of mammalian endoplasmic reticulum P450 proteins. Mol. Pharmacol. 67 (2005), 1460–1469.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1460-1469
    • Liao, M.1    Zgoda, V.G.2    Murray, B.P.3    Correia, M.A.4
  • 33
    • 0037413156 scopus 로고    scopus 로고
    • Subcellular localization of oxidosqualene cyclases from Arabidopsis thaliana, Trypanosoma cruzi, and Pneumocystis carinii expressed in yeast
    • Milla, P., Viola, F., Bosso, S.O., Rocco, F., Cattel, L., Joubert, B.M., LeClair, R.J., Matsuda, S.P.T., Balliano, G., Subcellular localization of oxidosqualene cyclases from Arabidopsis thaliana, Trypanosoma cruzi, and Pneumocystis carinii expressed in yeast. Lipids 37 (2002), 1171–1176.
    • (2002) Lipids , vol.37 , pp. 1171-1176
    • Milla, P.1    Viola, F.2    Bosso, S.O.3    Rocco, F.4    Cattel, L.5    Joubert, B.M.6    LeClair, R.J.7    Matsuda, S.P.T.8    Balliano, G.9
  • 35
    • 77953200019 scopus 로고    scopus 로고
    • Genomic and coexpression analyses predict multiple genes involved in triterpene saponin biosynthesis in Medicago truncatula
    • Naoumkina, M.A., Modolo, L.V., Huhman, D.V., Urbanczyk-Wochniak, E., Tang, Y., Sumner, L.W., Dixon, R.A., Genomic and coexpression analyses predict multiple genes involved in triterpene saponin biosynthesis in Medicago truncatula. Plant Cell. 22 (2010), 850–866.
    • (2010) Plant Cell. , vol.22 , pp. 850-866
    • Naoumkina, M.A.1    Modolo, L.V.2    Huhman, D.V.3    Urbanczyk-Wochniak, E.4    Tang, Y.5    Sumner, L.W.6    Dixon, R.A.7
  • 36
    • 0019421720 scopus 로고
    • Subcellular localization of the enzymes involved in the late stage of ergosterol biosynthesis in yeast
    • Nishino, T., Hata, S., Taketani, S., Yabusaki, Y., Katsuki, H., Subcellular localization of the enzymes involved in the late stage of ergosterol biosynthesis in yeast. J. Biochem. 89 (1981), 1391–1396.
    • (1981) J. Biochem. , vol.89 , pp. 1391-1396
    • Nishino, T.1    Hata, S.2    Taketani, S.3    Yabusaki, Y.4    Katsuki, H.5
  • 37
    • 34247099779 scopus 로고    scopus 로고
    • Functional analysis of Arabidopsis thaliana RHM2/MUM4, a multidomain protein involved in UDP-D-glucose to UDP-L-rhamnose conversion
    • Oka, T., Nemoto, T., Jigami, Y., Functional analysis of Arabidopsis thaliana RHM2/MUM4, a multidomain protein involved in UDP-D-glucose to UDP-L-rhamnose conversion. J. Biol. Chem. 282 (2007), 5389–5403.
    • (2007) J. Biol. Chem. , vol.282 , pp. 5389-5403
    • Oka, T.1    Nemoto, T.2    Jigami, Y.3
  • 38
    • 84872377725 scopus 로고    scopus 로고
    • Carotenoid-based phenotypic screen of the yeast deletion collection reveals new genes with roles in isoprenoid production
    • Özaydın, B., Burd, H., Lee, T., Keasling, J.D., Carotenoid-based phenotypic screen of the yeast deletion collection reveals new genes with roles in isoprenoid production. Metab. Eng. 15 (2013), 174–183.
    • (2013) Metab. Eng. , vol.15 , pp. 174-183
    • Özaydın, B.1    Burd, H.2    Lee, T.3    Keasling, J.D.4
  • 40
    • 34347392289 scopus 로고    scopus 로고
    • The structure and function of Saccharomyces cerevisiae proteinase A
    • Parr, C.L., Keates, R.A.B., Bryksa, B.C., Ogawa, M., Yada, R.Y., The structure and function of Saccharomyces cerevisiae proteinase A. Yeast 24 (2007), 467–480.
    • (2007) Yeast , vol.24 , pp. 467-480
    • Parr, C.L.1    Keates, R.A.B.2    Bryksa, B.C.3    Ogawa, M.4    Yada, R.Y.5
  • 41
    • 84873658613 scopus 로고    scopus 로고
    • Malaria drug made in yeast causes market ferment
    • Peplow, M., Malaria drug made in yeast causes market ferment. Nature 494 (2013), 160–161.
    • (2013) Nature , vol.494 , pp. 160-161
    • Peplow, M.1
  • 42
    • 84897553187 scopus 로고    scopus 로고
    • Cytochrome P450-mediated metabolic engineering: current progress and future challenges
    • Renault, H., Bassard, J.-E., Hamberger, B., Werck-Reichhart, D., Cytochrome P450-mediated metabolic engineering: current progress and future challenges. Curr. Opin. Plant Biol. 19 (2014), 27–34.
    • (2014) Curr. Opin. Plant Biol. , vol.19 , pp. 27-34
    • Renault, H.1    Bassard, J.-E.2    Hamberger, B.3    Werck-Reichhart, D.4
  • 43
    • 0036918780 scopus 로고    scopus 로고
    • Cloning, functional expression, and subcellular localization of multiple NADPH-cytochrome P450 reductases from hybrid poplar
    • Ro, D.-K., Ehlting, J., Douglas, C.J., Cloning, functional expression, and subcellular localization of multiple NADPH-cytochrome P450 reductases from hybrid poplar. Plant Physiol. 130 (2002), 1837–1851.
    • (2002) Plant Physiol. , vol.130 , pp. 1837-1851
    • Ro, D.-K.1    Ehlting, J.2    Douglas, C.J.3
  • 45
    • 0034965835 scopus 로고    scopus 로고
    • Functional characterization and subcellular localization of poplar (Populus trichocarpa x Populus deltoides) cinnamate 4-hydroxylase
    • Ro, D.K., Mah, N., Ellis, B.E., Douglas, C.J., Functional characterization and subcellular localization of poplar (Populus trichocarpa x Populus deltoides) cinnamate 4-hydroxylase. Plant Physiol. 126 (2001), 317–329.
    • (2001) Plant Physiol. , vol.126 , pp. 317-329
    • Ro, D.K.1    Mah, N.2    Ellis, B.E.3    Douglas, C.J.4
  • 46
    • 21244480972 scopus 로고    scopus 로고
    • The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth
    • Santos-Rosa, H., Leung, J., Grimsey, N., Peak-Chew, S., Siniossoglou, S., The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth. EMBO J. 24 (2005), 1931–1941.
    • (2005) EMBO J. , vol.24 , pp. 1931-1941
    • Santos-Rosa, H.1    Leung, J.2    Grimsey, N.3    Peak-Chew, S.4    Siniossoglou, S.5
  • 47
    • 84939528950 scopus 로고    scopus 로고
    • P450s and UGTs: key players in the structural diversity of triterpenoid saponins
    • Seki, H., Tamura, K., Muranaka, T., P450s and UGTs: key players in the structural diversity of triterpenoid saponins. Plant Cell Physiol. 56 (2015), 1463–1471.
    • (2015) Plant Cell Physiol. , vol.56 , pp. 1463-1471
    • Seki, H.1    Tamura, K.2    Muranaka, T.3
  • 48
    • 33847378479 scopus 로고    scopus 로고
    • Engineering of the pyruvate dehydrogenase bypass in Saccharomyces cerevisiae for high-level production of isoprenoids
    • Shiba, Y., Paradise, E.M., Kirby, J., Ro, D.-K., Keasing, J.D., Engineering of the pyruvate dehydrogenase bypass in Saccharomyces cerevisiae for high-level production of isoprenoids. Metab. Eng. 9 (2007), 160–168.
    • (2007) Metab. Eng. , vol.9 , pp. 160-168
    • Shiba, Y.1    Paradise, E.M.2    Kirby, J.3    Ro, D.-K.4    Keasing, J.D.5
  • 49
    • 84918823723 scopus 로고    scopus 로고
    • Identification of novel knockout targets for improving terpenoids biosynthesis in Saccharomyces cerevisiae
    • Sun, Z., Meng, H., Li, J., Wang, J., Li, Q., Wang, Y., Zhang, Y., Identification of novel knockout targets for improving terpenoids biosynthesis in Saccharomyces cerevisiae. PLoS One, 9, 2014, e112615.
    • (2014) PLoS One , vol.9 , pp. e112615
    • Sun, Z.1    Meng, H.2    Li, J.3    Wang, J.4    Li, Q.5    Wang, Y.6    Zhang, Y.7
  • 52
    • 0028357263 scopus 로고
    • Characterization of recombinant plant cinnamate 4-hydroxylase produced in yeast - Kinetic and spectral properties of the major plant P450 of the phenylpropanoid pathway
    • Urban, P., Werckreichhart, D., Teutsch, H.G., Durst, F., Regnier, S., Kazmaier, M., Pompon, D., Characterization of recombinant plant cinnamate 4-hydroxylase produced in yeast - Kinetic and spectral properties of the major plant P450 of the phenylpropanoid pathway. Eur. J. Biochem. 222 (1994), 843–850.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 843-850
    • Urban, P.1    Werckreichhart, D.2    Teutsch, H.G.3    Durst, F.4    Regnier, S.5    Kazmaier, M.6    Pompon, D.7
  • 54
    • 0029679761 scopus 로고    scopus 로고
    • Vacuolar and extracellular maturation of Saccharomyces cerevisiae proteinase A
    • Wolff, A.M., Din, N., Petersen, J.G.L., Vacuolar and extracellular maturation of Saccharomyces cerevisiae proteinase A. Yeast 12 (1996), 823–832.
    • (1996) Yeast , vol.12 , pp. 823-832
    • Wolff, A.M.1    Din, N.2    Petersen, J.G.L.3
  • 55
    • 0034677907 scopus 로고    scopus 로고
    • Biochemical characterization and subcellular localization of the sterol C-24(28) reductase, Erg4p, from the yeast Saccharomyces cerevisiae
    • Zweytick, D., Hrastnik, C., Kohlwein, S.D., Daum, G., Biochemical characterization and subcellular localization of the sterol C-24(28) reductase, Erg4p, from the yeast Saccharomyces cerevisiae. FEBS Lett. 470 (2000), 83–87.
    • (2000) FEBS Lett. , vol.470 , pp. 83-87
    • Zweytick, D.1    Hrastnik, C.2    Kohlwein, S.D.3    Daum, G.4


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