메뉴 건너뛰기




Volumn 262, Issue 4-5, 1999, Pages 857-868

Analysis of β-tubulin cDNAs from taxol-resistant Pestalotiopsis microspora and taxol-sensitive Pythium ultimum and comparison of the taxol-binding properties of their products

Author keywords

tubulin; Achlya klebsiana; Pestalotiopsis microspora; Pythium ultimum; Taxol

Indexed keywords

ANTINEOPLASTIC AGENT; ASPARAGINE; BETA TUBULIN; COMPLEMENTARY DNA; GLUTAMINE; PACLITAXEL; THREONINE; TIABENDAZOLE; TRITIUM;

EID: 0033376338     PISSN: 00268925     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004380051151     Document Type: Article
Times cited : (19)

References (50)
  • 1
    • 0027056174 scopus 로고
    • Yeast proteins associated with microtubules in vitro and in vivo
    • Barnes G, Louie KA, Botstein D (1992) Yeast proteins associated with microtubules in vitro and in vivo. Mol Biol Cell 3:29-47
    • (1992) Mol Biol Cell , vol.3 , pp. 29-47
    • Barnes, G.1    Louie, K.A.2    Botstein, D.3
  • 4
    • 0017602345 scopus 로고
    • Differential binding of methyl benzimidazole-2-yl-carbamate to fungal tubulin as a mechanism of resistance to this antimitotic agent in mutant strains of Aspergillus nidulans
    • Davidse LC, Flach W (1977) Differential binding of methyl benzimidazole-2-yl-carbamate to fungal tubulin as a mechanism of resistance to this antimitotic agent in mutant strains of Aspergillus nidulans. J Cell Biol 72:174-193
    • (1977) J Cell Biol , vol.72 , pp. 174-193
    • Davidse, L.C.1    Flach, W.2
  • 5
    • 0018163716 scopus 로고
    • Interaction of thiabendazole with fungal tubulin
    • Davidse LC, Flach W (1978) Interaction of thiabendazole with fungal tubulin. Biochim Biophys Acta 543:82-90
    • (1978) Biochim Biophys Acta , vol.543 , pp. 82-90
    • Davidse, L.C.1    Flach, W.2
  • 6
    • 0019472440 scopus 로고
    • Molecular analysis of cytoplasmic microtubules in situ: Identification of both widespread and specific proteins
    • Duerr A, Pallas D, Solomon F (1981) Molecular analysis of cytoplasmic microtubules in situ: identification of both widespread and specific proteins. Cell 24:203-211
    • (1981) Cell , vol.24 , pp. 203-211
    • Duerr, A.1    Pallas, D.2    Solomon, F.3
  • 7
    • 0026783544 scopus 로고
    • Site-directed mutagenesis of the GTP-binding domain of β-tubulin
    • Farr GW, Sternlicht H (1992) Site-directed mutagenesis of the GTP-binding domain of β-tubulin. J Mol Biol 227:307-321
    • (1992) J Mol Biol , vol.227 , pp. 307-321
    • Farr, G.W.1    Sternlicht, H.2
  • 8
    • 0026559290 scopus 로고
    • A single amino-acid substitution in the beta-tubulin gene of Neurospora confers both cabendazim resistance and diethofencarb sensitivity
    • Fugimura M, Oeda K, Inoue H, Kato T (1992) A single amino-acid substitution in the beta-tubulin gene of Neurospora confers both cabendazim resistance and diethofencarb sensitivity. Curr Genet 21:399-404
    • (1992) Curr Genet , vol.21 , pp. 399-404
    • Fugimura, M.1    Oeda, K.2    Inoue, H.3    Kato, T.4
  • 9
    • 0030758777 scopus 로고    scopus 로고
    • Paclitaxel-resistant human ovarian cancer cells have mutant β-tubulins that exhibit impaired paclitaxel-driven polymerization
    • Giannakakou P, Sackett DL, Kang Y-K, Zhan Z, Buters JTM, Fojo T, Poruchynsky MS (1997) Paclitaxel-resistant human ovarian cancer cells have mutant β-tubulins that exhibit impaired paclitaxel-driven polymerization. J Biol Chem 272:17118-17125
    • (1997) J Biol Chem , vol.272 , pp. 17118-17125
    • Giannakakou, P.1    Sackett, D.L.2    Kang, Y.-K.3    Zhan, Z.4    Buters, J.T.M.5    Fojo, T.6    Poruchynsky, M.S.7
  • 10
    • 0027234352 scopus 로고
    • A nucleotide substitution in one of the β-tubulin genes of Trichoderma viride confers resistance to the antimitotic drug methyl benzimidazole-2-yl-carbamate
    • Goldman GH, Temmerman W, Jacobs D, Contreras R, Van Montagu M, Herrera-Estrella A (1993) A nucleotide substitution in one of the β-tubulin genes of Trichoderma viride confers resistance to the antimitotic drug methyl benzimidazole-2-yl-carbamate. Mol Gen Genet 240:73-80
    • (1993) Mol Gen Genet , vol.240 , pp. 73-80
    • Goldman, G.H.1    Temmerman, W.2    Jacobs, D.3    Contreras, R.4    Van Montagu, M.5    Herrera-Estrella, A.6
  • 11
    • 0021716157 scopus 로고
    • The NDA3 gene of fission yeast encodes β-tubulin: A cold-sensitive nda3 mutation reversibly blocks spindle formation and chromosome movement in mitosis
    • Hiraoka Y, Toda T, Yanagida M (1984) The NDA3 gene of fission yeast encodes β-tubulin: a cold-sensitive nda3 mutation reversibly blocks spindle formation and chromosome movement in mitosis. Cell 39:349-358
    • (1984) Cell , vol.39 , pp. 349-358
    • Hiraoka, Y.1    Toda, T.2    Yanagida, M.3
  • 12
    • 0026516994 scopus 로고
    • Mechanism of action of taxol
    • Horwitz SB (1992) Mechanism of action of taxol. Trends Pharmacol Sci 13:134-136
    • (1992) Trends Pharmacol Sci , vol.13 , pp. 134-136
    • Horwitz, S.B.1
  • 13
    • 0027533571 scopus 로고
    • Restoration of taxol sensitivity of multidrug-resistant cells by the cyclosporine SDZ PSC 833 and the cyclopeptide SDZ 280-446
    • Jachez B, Nordmann R, Loor F (1993) Restoration of taxol sensitivity of multidrug-resistant cells by the cyclosporine SDZ PSC 833 and the cyclopeptide SDZ 280-446. J Natl Cancer Inst 85:478-483
    • (1993) J Natl Cancer Inst , vol.85 , pp. 478-483
    • Jachez, B.1    Nordmann, R.2    Loor, F.3
  • 14
    • 0025066572 scopus 로고
    • Identification of an amino acid substitution in the benA, β-tubulin gene of Aspergillus nidulans that confers thiabendazole resistance and benomyl supersensitivity
    • Jung MK, Oakley BR (1990) Identification of an amino acid substitution in the benA, β-tubulin gene of Aspergillus nidulans that confers thiabendazole resistance and benomyl supersensitivity. Cell Motil Cytoskeleton 17:87-94
    • (1990) Cell Motil Cytoskeleton , vol.17 , pp. 87-94
    • Jung, M.K.1    Oakley, B.R.2
  • 15
    • 0026708525 scopus 로고
    • Amino acid alterations in the benA (β-tubulin) gene of Aspergillus nidulans that confer benomyl resistance
    • Jung MK, Wilder IB, Oakley BR (1992) Amino acid alterations in the benA (β-tubulin) gene of Aspergillus nidulans that confer benomyl resistance. Cell Motil Cytoskeleton 22:170-174
    • (1992) Cell Motil Cytoskeleton , vol.22 , pp. 170-174
    • Jung, M.K.1    Wilder, I.B.2    Oakley, B.R.3
  • 16
    • 0024843620 scopus 로고
    • Proteins in the centrosome, spindle, and kinetochore of the early Drosophila embryo
    • Kellogg DR, Field CM, Alberts BM (1989) Proteins in the centrosome, spindle, and kinetochore of the early Drosophila embryo. J Cell Biol 109:2977-2991
    • (1989) J Cell Biol , vol.109 , pp. 2977-2991
    • Kellogg, D.R.1    Field, C.M.2    Alberts, B.M.3
  • 17
    • 0019876086 scopus 로고
    • Purification of yeast tubulin by self-assembly in vitro
    • Kilmartin JV (1981) Purification of yeast tubulin by self-assembly in vitro. Biochemistry 20:3629-3633
    • (1981) Biochemistry , vol.20 , pp. 3629-3633
    • Kilmartin, J.V.1
  • 18
    • 0029824617 scopus 로고    scopus 로고
    • Endophytic taxol-producing fungi from bald cypress, Taxodium distichum
    • Li J-Y, Strobel G, Sidhu R, Hess WM, Ford EJ (1996) Endophytic taxol-producing fungi from bald cypress, Taxodium distichum. Microbiology 142:223-226
    • (1996) Microbiology , vol.142 , pp. 223-226
    • Li, J.-Y.1    Strobel, G.2    Sidhu, R.3    Hess, W.M.4    Ford, E.J.5
  • 19
    • 0031843384 scopus 로고    scopus 로고
    • Stimulation of taxol production in liquid culture of Pestalotiopsis microspora
    • Li J-Y, Sidhu RS, Bollon A, Strobel GA (1998a) Stimulation of taxol production in liquid culture of Pestalotiopsis microspora. Mycol Res 102:461-464
    • (1998) Mycol Res , vol.102 , pp. 461-464
    • Li, J.-Y.1    Sidhu, R.S.2    Bollon, A.3    Strobel, G.A.4
  • 21
    • 0023754156 scopus 로고
    • The GTP-binding peptide of β-tubulin: Localization by direct photoaffinity labeling and comparison with nucleotide-binding proteins
    • Linse K, Mandelkow E-M (1988) The GTP-binding peptide of β-tubulin: localization by direct photoaffinity labeling and comparison with nucleotide-binding proteins. J Biol Chem 263:15205-15210
    • (1988) J Biol Chem , vol.263 , pp. 15205-15210
    • Linse, K.1    Mandelkow, E.-M.2
  • 24
    • 0021229643 scopus 로고
    • Taxol: An antimitotic agent with a new mechanism of action
    • Manfredi JJ, Horwitz SB (1984) Taxol: an antimitotic agent with a new mechanism of action. Pharmacol Ther 25:83-125
    • (1984) Pharmacol Ther , vol.25 , pp. 83-125
    • Manfredi, J.J.1    Horwitz, S.B.2
  • 26
    • 0023064410 scopus 로고
    • Aspergillus nidulans β-tubulin genes are usually divergent
    • May GS, Tsang ML-S, Smith H, Fidel S, Morris NR (1987) Aspergillus nidulans β-tubulin genes are usually divergent. Gene 55:231-243
    • (1987) Gene , vol.55 , pp. 231-243
    • May, G.S.1    Tsang, M.L.-S.2    Smith, H.3    Fidel, S.4    Morris, N.R.5
  • 27
    • 0020600632 scopus 로고
    • Isolation of the β-tubulin gene from yeast and demonstration of its essential function in vivo
    • Neff NF, Thomas JH, Grisafi P, Botstein D (1983) Isolation of the β-tubulin gene from yeast and demonstration of its essential function in vivo. Cell 33:211-219
    • (1983) Cell , vol.33 , pp. 211-219
    • Neff, N.F.1    Thomas, J.H.2    Grisafi, P.3    Botstein, D.4
  • 28
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the αβ tubulin dimer by electron crystallography
    • Nogales E, Wolf SG, Downing KH (1998) Structure of the αβ tubulin dimer by electron crystallography. Nature 391:199-203
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 30
    • 0002641926 scopus 로고
    • Gamma-tubulin
    • Hyams JS, Lloyd CW (eds). Wiley-Liss, New York
    • Oakley BR (1994) Gamma-tubulin. In: Hyams JS, Lloyd CW (eds) Microtubules. Wiley-Liss, New York, pp 38-45
    • (1994) Microtubules , pp. 38-45
    • Oakley, B.R.1
  • 31
    • 0022751236 scopus 로고
    • Cloning and characterization of the gene for β-tubulin from a benomyl-resistant mutant of Neurospora crassa and its use as a dominant selectable marker
    • Orbach MJ, Porro EB, Yanofsky C (1986) Cloning and characterization of the gene for β-tubulin from a benomyl-resistant mutant of Neurospora crassa and its use as a dominant selectable marker. Mol Cell Biol 6:2452-2461
    • (1986) Mol Cell Biol , vol.6 , pp. 2452-2461
    • Orbach, M.J.1    Porro, E.B.2    Yanofsky, C.3
  • 32
    • 0000215868 scopus 로고
    • Colletotrichum graminicola transformed with homologous and heterologous benomyl-resistance genes retains expected pathogenicity to corn
    • Panaccione DG, McKiernan M, Hanau RM (1988) Colletotrichum graminicola transformed with homologous and heterologous benomyl-resistance genes retains expected pathogenicity to corn. Mol Plant Microbe Interact 1:113-120
    • (1988) Mol Plant Microbe Interact , vol.1 , pp. 113-120
    • Panaccione, D.G.1    McKiernan, M.2    Hanau, R.M.3
  • 33
    • 0019859353 scopus 로고
    • Taxol binds to polymerized tubulin in vitro
    • Parness J, Horwitz SB (1981) Taxol binds to polymerized tubulin in vitro. J Cell Biol 91:479-487
    • (1981) J Cell Biol , vol.91 , pp. 479-487
    • Parness, J.1    Horwitz, S.B.2
  • 34
    • 0017089669 scopus 로고
    • 3′ Non-coding region sequences in eukaryotic messenger RNA
    • Proudfoot NJ, Brownlee GG (1976) 3′ Non-coding region sequences in eukaryotic messenger RNA. Nature 263:211-214
    • (1976) Nature , vol.263 , pp. 211-214
    • Proudfoot, N.J.1    Brownlee, G.G.2
  • 37
    • 0026345003 scopus 로고
    • The clinical pharmacology and use of antimicrotubule agents in cancer chemotherapeutics
    • Rowinsky EK, Donehower RC (1991) The clinical pharmacology and use of antimicrotubule agents in cancer chemotherapeutics. Pharmacol Ther 52:35-84
    • (1991) Pharmacol Ther , vol.52 , pp. 35-84
    • Rowinsky, E.K.1    Donehower, R.C.2
  • 39
    • 0018387446 scopus 로고
    • Promotion of microtubule assembly in vitro by taxol
    • Schiff PB, Fant J, Horwitz SB (1979) Promotion of microtubule assembly in vitro by taxol. Nature 277:665-667
    • (1979) Nature , vol.277 , pp. 665-667
    • Schiff, P.B.1    Fant, J.2    Horwitz, S.B.3
  • 40
    • 0019585912 scopus 로고
    • Stabilization of the cytoplasmic ground substance in detergent-opened cells and a structural and biochemical analysis of its composition
    • Schliwa M, van Blerkom J, Porter KR (1981) Stabilization of the cytoplasmic ground substance in detergent-opened cells and a structural and biochemical analysis of its composition. Proc Natl Acad Sci USA 78:4329-4333
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 4329-4333
    • Schliwa, M.1    Van Blerkom, J.2    Porter, K.R.3
  • 41
    • 0027270462 scopus 로고
    • Taxol and taxane production by Taxomyces andreanae, an endophytic fungus of Pacific yew
    • Stierle A, Strobel G, Stierle D (1993) Taxol and taxane production by Taxomyces andreanae, an endophytic fungus of Pacific yew. Science 260:214-216
    • (1993) Science , vol.260 , pp. 214-216
    • Stierle, A.1    Strobel, G.2    Stierle, D.3
  • 43
    • 0030059628 scopus 로고    scopus 로고
    • Taxol from Pestalotiopsis microspora, an endophytic fungus of Taxus wallachiana
    • Strobel G, Yang X, Sears J, Kramer R, Sidhu RS, Hess WM (1996b) Taxol from Pestalotiopsis microspora, an endophytic fungus of Taxus wallachiana. Microbiology 142:435-440
    • (1996) Microbiology , vol.142 , pp. 435-440
    • Strobel, G.1    Yang, X.2    Sears, J.3    Kramer, R.4    Sidhu, R.S.5    Hess, W.M.6
  • 44
    • 0024151129 scopus 로고
    • Structure and utilization of tubulin isotypes
    • Sullivan KF (1988) Structure and utilization of tubulin isotypes. Ann Rev Cell Biol 4:687-716
    • (1988) Ann Rev Cell Biol , vol.4 , pp. 687-716
    • Sullivan, K.F.1
  • 45
    • 0022408888 scopus 로고
    • Isolation and characterization of mutations in the β-tubulin gene of Saccharomyces cerevisiae
    • Thomas JH, Neff NF, Botstein D (1985) Isolation and characterization of mutations in the β-tubulin gene of Saccharomyces cerevisiae. Genetics 112:715-734
    • (1985) Genetics , vol.112 , pp. 715-734
    • Thomas, J.H.1    Neff, N.F.2    Botstein, D.3
  • 46
    • 0015211527 scopus 로고
    • Plant antitumor agents. VI. The isolation and structure of taxol, a novel antileukemic and antitumor agent from Taxus brevifolia
    • Wani MC, Taylor HL, Wall ME, Coggon P, McPhail AT (1971) Plant antitumor agents. VI. The isolation and structure of taxol, a novel antileukemic and antitumor agent from Taxus brevifolia. J Am Chem Soc 93:2325-2327
    • (1971) J Am Chem Soc , vol.93 , pp. 2325-2327
    • Wani, M.C.1    Taylor, H.L.2    Wall, M.E.3    Coggon, P.4    McPhail, A.T.5
  • 48
    • 0024291284 scopus 로고
    • Autoregulated instability of β-tubulin mRNAs by recognition of the nascent amino terminus of β-tubulin
    • Yen TJ, Machlin PS, Cleveland DW (1988) Autoregulated instability of β-tubulin mRNAs by recognition of the nascent amino terminus of β-tubulin. Nature 334:580-585
    • (1988) Nature , vol.334 , pp. 580-585
    • Yen, T.J.1    Machlin, P.S.2    Cleveland, D.W.3
  • 49
    • 0029024874 scopus 로고
    • Purification and characterization of assembly-competent tubulin from Aspergillus nidulans
    • Yoon Y, Oakley BR (1995) Purification and characterization of assembly-competent tubulin from Aspergillus nidulans. Biochemistry 34:6373-6381
    • (1995) Biochemistry , vol.34 , pp. 6373-6381
    • Yoon, Y.1    Oakley, B.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.