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Volumn 1625, Issue 2, 2003, Pages 134-140

Isolation and characterization of four cell wall purple acid phosphatase genes from tobacco cells

Author keywords

Cell wall enzyme; Cell wall regeneration; Gene expression; Nicotiana tabacum; Protoplast; Purple acid phosphatase

Indexed keywords

ACID PHOSPHATASE TARTRATE RESISTANT ISOENZYME; COMPLEMENTARY DNA; GENE PRODUCT; MESSENGER RNA;

EID: 0037467680     PISSN: 01674781     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4781(02)00599-7     Document Type: Article
Times cited : (20)

References (40)
  • 1
    • 0000651436 scopus 로고
    • The protein component of primary cell walls
    • Preston R.D. New York: Academic Press
    • Lamport D.T.A. The protein component of primary cell walls. Preston R.D. Advances in Botanical Research. vol. 2:1965;151-218 Academic Press, New York.
    • (1965) Advances in Botanical Research , vol.2 , pp. 151-218
    • Lamport, D.T.A.1
  • 3
    • 0028878632 scopus 로고
    • Polysaccharide-modifying enzymes in the plant cell wall
    • Fry S.C. Polysaccharide-modifying enzymes in the plant cell wall. Annu. Rev. Plant Physiol. Plant Mol. Biol. 46:1995;497-520.
    • (1995) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.46 , pp. 497-520
    • Fry, S.C.1
  • 4
    • 0031439907 scopus 로고    scopus 로고
    • Assembly and enlargement of the primary cell wall in plants
    • Cosgrove D.J. Assembly and enlargement of the primary cell wall in plants. Annu. Rev. Cell Dev. Biol. 13:1997;171-201.
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 171-201
    • Cosgrove, D.J.1
  • 5
    • 0012493842 scopus 로고
    • Release of enzymes by plant tissue cultures
    • Straus J., Campbell W.A. Release of enzymes by plant tissue cultures. Life Sci. 1:1963;50-62.
    • (1963) Life Sci. , vol.1 , pp. 50-62
    • Straus, J.1    Campbell, W.A.2
  • 7
    • 0012490732 scopus 로고
    • Cell-wall column chromatographic identification of the native cell-wall acid phosphatase of cultured tobacco cells
    • Suzuki T., Sato S. Cell-wall column chromatographic identification of the native cell-wall acid phosphatase of cultured tobacco cells. Plant Cell Physiol. 17:1976;847-849.
    • (1976) Plant Cell Physiol. , vol.17 , pp. 847-849
    • Suzuki, T.1    Sato, S.2
  • 8
    • 84982740683 scopus 로고
    • Purification and molecular properties of acid phosphatase from sycamore cell walls
    • Crasnier M., Noat G., Ricard J. Purification and molecular properties of acid phosphatase from sycamore cell walls. Plant Cell Environ. 3:1980;217-224.
    • (1980) Plant Cell Environ. , vol.3 , pp. 217-224
    • Crasnier, M.1    Noat, G.2    Ricard, J.3
  • 9
    • 0001081456 scopus 로고
    • Resolution and some properties of acid phosphatase isozymes bound to the cell wall of potato tubers
    • Sugawara S., Inamoto Y., Ushijima M. Resolution and some properties of acid phosphatase isozymes bound to the cell wall of potato tubers. Agric. Biol. Chem. 45:1981;1767-1773.
    • (1981) Agric. Biol. Chem. , vol.45 , pp. 1767-1773
    • Sugawara, S.1    Inamoto, Y.2    Ushijima, M.3
  • 10
    • 0002927428 scopus 로고
    • Effects of multivalent cations on cell wall-associated acid phosphatase activity
    • Tu S.I., Brouillette J.N., Nagahashi G., Kumosinski T.F. Effects of multivalent cations on cell wall-associated acid phosphatase activity. Plant Physiol. 88:1988;61-68.
    • (1988) Plant Physiol. , vol.88 , pp. 61-68
    • Tu, S.I.1    Brouillette, J.N.2    Nagahashi, G.3    Kumosinski, T.F.4
  • 11
    • 0000213361 scopus 로고
    • Purification and characterization of secreted purple phosphatase from soybean suspension cultures
    • LeBansky B.R., McKnight T.D., Griffing L.R. Purification and characterization of secreted purple phosphatase from soybean suspension cultures. Plant Physiol. 99:1992;391-395.
    • (1992) Plant Physiol. , vol.99 , pp. 391-395
    • LeBansky, B.R.1    McKnight, T.D.2    Griffing, L.R.3
  • 12
    • 0001682590 scopus 로고
    • Phosphatase starvation inducible metabolism in Lycopersicon esculentum
    • Goldstein A.H., Baertlein D.A., McDaniel R.G. Phosphatase starvation inducible metabolism in Lycopersicon esculentum. Plant Physiol. 87:1988;711-715.
    • (1988) Plant Physiol. , vol.87 , pp. 711-715
    • Goldstein, A.H.1    Baertlein, D.A.2    McDaniel, R.G.3
  • 13
    • 84982663409 scopus 로고
    • Phosphate influx and extracellular phosphatase activity in barley roots and rose cells
    • Lee R.B. Phosphate influx and extracellular phosphatase activity in barley roots and rose cells. New Phytol. 109:1988;141-148.
    • (1988) New Phytol. , vol.109 , pp. 141-148
    • Lee, R.B.1
  • 14
    • 0034781532 scopus 로고    scopus 로고
    • Molecular control of acid phosphatase secretion into the rhizosphere of proteoid roots from phosphorus-stressed white lupin
    • Miller S.S., Liu J., Allan D.L., Menzhuber C.J., Fedorova M., Vance C.P. Molecular control of acid phosphatase secretion into the rhizosphere of proteoid roots from phosphorus-stressed white lupin. Plant Physiol. 127:2001;594-606.
    • (2001) Plant Physiol. , vol.127 , pp. 594-606
    • Miller, S.S.1    Liu, J.2    Allan, D.L.3    Menzhuber, C.J.4    Fedorova, M.5    Vance, C.P.6
  • 17
    • 0029640070 scopus 로고
    • Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site
    • Sträter N., Klabunde T., Tucker P., Witzel H., Krebs B. Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site. Science. 268:1995;1489-1492.
    • (1995) Science , vol.268 , pp. 1489-1492
    • Sträter, N.1    Klabunde, T.2    Tucker, P.3    Witzel, H.4    Krebs, B.5
  • 18
    • 0030596529 scopus 로고    scopus 로고
    • Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structure
    • Klabunde T., Sträter N., Fröhlich R., Witzel H., Krebs B. Mechanism of Fe(III)-Zn(II) purple acid phosphatase based on crystal structure. J. Mol. Biol. 259:1996;737-748.
    • (1996) J. Mol. Biol. , vol.259 , pp. 737-748
    • Klabunde, T.1    Sträter, N.2    Fröhlich, R.3    Witzel, H.4    Krebs, B.5
  • 19
    • 0000396193 scopus 로고
    • Purification and properties of native cell wall acid phosphatase from cultured tobacco cells
    • Kaneko T.S., Kikuti R., Kubota K. Purification and properties of native cell wall acid phosphatase from cultured tobacco cells. Phytochemistry. 29:1990;2883-2887.
    • (1990) Phytochemistry , vol.29 , pp. 2883-2887
    • Kaneko, T.S.1    Kikuti, R.2    Kubota, K.3
  • 20
    • 0012542761 scopus 로고
    • Inhibitory effect of brefeldine A on cell wall generation of tobacco protoplasts
    • Kaneko T.S., Terasawa N. Inhibitory effect of brefeldine A on cell wall generation of tobacco protoplasts. J. Jpn. Women's Univ. Fac. Sci. 1:1993;59-62.
    • (1993) J. Jpn. Women's Univ. Fac. Sci. , vol.1 , pp. 59-62
    • Kaneko, T.S.1    Terasawa, N.2
  • 21
    • 0030040027 scopus 로고    scopus 로고
    • Two isoforms of acid phosphatase secreted by tobacco protoplasts: Differential effect of brefeldin A on their secretion
    • Kaneko T.S., Sato M., Osumi M., Muroi M., Takatsuki A. Two isoforms of acid phosphatase secreted by tobacco protoplasts: differential effect of brefeldin A on their secretion. Plant Cell Rep. 15:1996;409-413.
    • (1996) Plant Cell Rep. , vol.15 , pp. 409-413
    • Kaneko, T.S.1    Sato, M.2    Osumi, M.3    Muroi, M.4    Takatsuki, A.5
  • 22
    • 0032145880 scopus 로고    scopus 로고
    • 60 kD polypeptide of cell wall acid phosphatase from tobacco cells
    • Kaneko T.S., Kuwabara C., Tomioka S., Suzuki K. 60 kD polypeptide of cell wall acid phosphatase from tobacco cells. Phytochemistry. 48:1998;1125-1130.
    • (1998) Phytochemistry , vol.48 , pp. 1125-1130
    • Kaneko, T.S.1    Kuwabara, C.2    Tomioka, S.3    Suzuki, K.4
  • 23
    • 0012546508 scopus 로고    scopus 로고
    • Plant cell wall acid phosphatase
    • Kaneko T.S. Plant cell wall acid phosphatase. Curr. Top. Plant Biol. 1:1999;105-111.
    • (1999) Curr. Top. Plant Biol. , vol.1 , pp. 105-111
    • Kaneko, T.S.1
  • 25
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue culture
    • Murashige T., Skoog F. A revised medium for rapid growth and bioassays with tobacco tissue culture. Physiol. Plant. 15:1962;473-497.
    • (1962) Physiol. Plant. , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 26
    • 0000917687 scopus 로고
    • Regulation of phosphatase synthesis by orthophosphate in cultured tobacco cells
    • Ueki K., Sato S. Regulation of phosphatase synthesis by orthophosphate in cultured tobacco cells. Plant Cell Physiol. 18:1977;1253-1263.
    • (1977) Plant Cell Physiol. , vol.18 , pp. 1253-1263
    • Ueki, K.1    Sato, S.2
  • 27
    • 0000155229 scopus 로고
    • Phenol/SDS method for plant RNA preparation
    • F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, & K. Struhl. New York: Wiley
    • Kingston R.E., Chomczynski P., Sacchi N. Phenol/SDS method for plant RNA preparation. Ausubel F.M., Brent R., Kingston R.E., Moore D.D., Seidman J.G., Smith J.A., Struhl K. Short Protocols in Molecular Biology. 3rd ed. 1995;4-7 Wiley, New York.
    • (1995) Short Protocols in Molecular Biology 3rd ed. , pp. 4-7
    • Kingston, R.E.1    Chomczynski, P.2    Sacchi, N.3
  • 28
    • 0015356037 scopus 로고
    • Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid cellulose
    • Aviv H., Leder P. Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid cellulose. Proc. Natl. Acad. Sci. U. S. A. 69:1972;1408-1412.
    • (1972) Proc. Natl. Acad. Sci. U. S. A. , vol.69 , pp. 1408-1412
    • Aviv, H.1    Leder, P.2
  • 29
    • 0034816542 scopus 로고    scopus 로고
    • Cloning and characterization of cDNA of the GPI-anchored purple acid phosphatase and its roots tissue distribution in Spirodela oligorrhiza
    • Nishikoori M., Washio K., Hase A., Morita N., Okuyama H. Cloning and characterization of cDNA of the GPI-anchored purple acid phosphatase and its roots tissue distribution in Spirodela oligorrhiza. Physiol. Plant. 113:2001;241-248.
    • (2001) Physiol. Plant. , vol.113 , pp. 241-248
    • Nishikoori, M.1    Washio, K.2    Hase, A.3    Morita, N.4    Okuyama, H.5
  • 30
    • 0023739575 scopus 로고
    • Regulation of Mu element copy number in maize lines with an active or inactive Mutator transposable element system
    • Walbot V., Warren C. Regulation of Mu element copy number in maize lines with an active or inactive Mutator transposable element system. MGG, Mol. Gen. Genet. 211:1988;27-34.
    • (1988) MGG, Mol. Gen. Genet. , vol.211 , pp. 27-34
    • Walbot, V.1    Warren, C.2
  • 31
    • 0001368223 scopus 로고
    • Cell wall regeneration and cell division in isolated tobacco mesophyll protoplast
    • Nagata T., Takebe I. Cell wall regeneration and cell division in isolated tobacco mesophyll protoplast. Planta (Berl.). 92:1970;301-308.
    • (1970) Planta (Berl.) , vol.92 , pp. 301-308
    • Nagata, T.1    Takebe, I.2
  • 32
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:1982;105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 33
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., Heijine G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1997;1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Heijine, G.4
  • 35
    • 0032712080 scopus 로고    scopus 로고
    • Cloning and comparative protein modeling of two purple acid phosphatase isozymes from sweet potatoes (Ipomoea batatas)
    • Durmus A., Eicken C., Spener F., Krebs B. Cloning and comparative protein modeling of two purple acid phosphatase isozymes from sweet potatoes (Ipomoea batatas). Biochim. Biophys. Acta. 1434:1999;202-209.
    • (1999) Biochim. Biophys. Acta , vol.1434 , pp. 202-209
    • Durmus, A.1    Eicken, C.2    Spener, F.3    Krebs, B.4
  • 38
    • 0032990142 scopus 로고    scopus 로고
    • Structure of a cDNA for an acid phosphatase from phosphate-deficient lupin (Lupinus alubus L.) roots
    • Wasaki J., Omura M., Osaki M., Ito H., Matsui H., Shinano T., Tadano T. Structure of a cDNA for an acid phosphatase from phosphate-deficient lupin (Lupinus alubus L.) roots. Soil Sci. Plant Nutr. 45:1999;439-449.
    • (1999) Soil Sci. Plant Nutr. , vol.45 , pp. 439-449
    • Wasaki, J.1    Omura, M.2    Osaki, M.3    Ito, H.4    Matsui, H.5    Shinano, T.6    Tadano, T.7
  • 39
    • 0033559677 scopus 로고    scopus 로고
    • The active site of purple acid phosphatase from sweet potatoes (Ipomoea batatas) metal content and spectroscopic characterization
    • Durmus A., Eicken C., Sift B.H., Kratel A., Kappl R., Hüttermann J., Krebs B. The active site of purple acid phosphatase from sweet potatoes (Ipomoea batatas) metal content and spectroscopic characterization. Eur. J. Biochem. 260:1999;709-716.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 709-716
    • Durmus, A.1    Eicken, C.2    Sift, B.H.3    Kratel, A.4    Kappl, R.5    Hüttermann, J.6    Krebs, B.7


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