메뉴 건너뛰기




Volumn 31, Issue 3, 1996, Pages 465-478

A wound-inducible gene from Salix viminalis coding for a trypsin inhibitor

Author keywords

hypervariable region; Kunitz family; Salix viminalis; serine protease inhibitor; wound induced

Indexed keywords

ESCHERICHIA COLI; POPULUS; SALIX; SALIX VIMINALIS;

EID: 0030175102     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00042221     Document Type: Article
Times cited : (25)

References (53)
  • 1
    • 0026930761 scopus 로고
    • Intracellular trafficking of secretory proteins
    • Bednarek SY and Raikhel NV: Intracellular trafficking of secretory proteins. Plant Molecular biology 20: 133-150 (1992).
    • (1992) Plant Molecular Biology , vol.20 , pp. 133-150
    • Bednarek, S.Y.1    Raikhel, N.V.2
  • 2
    • 0001741062 scopus 로고
    • Genetics of actin-related sequences in tomato
    • Bernatzky R, Tanksley SD: Genetics of actin-related sequences in tomato. Theor Appl Genet 72: 314-321 (1986).
    • (1986) Theor Appl Genet , vol.72 , pp. 314-321
    • Bernatzky, R.1    Tanksley, S.D.2
  • 3
    • 0019518360 scopus 로고
    • Proteinase inhibitor inducing activity in tomato leaves resides in oligosaccharides enzymatically released from cell walls
    • Bishop PD, Markus DJ, Pearce G, Ryan CA: Proteinase inhibitor inducing activity in tomato leaves resides in oligosaccharides enzymatically released from cell walls. Proc Natl Acad Sci USA 78: 3536-3540 (1981).
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 3536-3540
    • Bishop, P.D.1    Markus, D.J.2    Pearce, G.3    Ryan, C.A.4
  • 4
    • 0024887875 scopus 로고
    • Use of cowpea trypsin inhibitor (CpTI) to protect plants against insect predation
    • Boulter D, Gatehouse AMR, Hilder V: Use of cowpea trypsin inhibitor (CpTI) to protect plants against insect predation. Biotech Adv 7: 489-497 (1989).
    • (1989) Biotech Adv , vol.7 , pp. 489-497
    • Boulter, D.1    Gatehouse, A.M.R.2    Hilder, V.3
  • 5
    • 0025252589 scopus 로고
    • Systemically wound-responsive genes in poplar trees encode proteins similar to sweet potato sporamins and legume Kunitz trypsin inhibitors
    • Bradshaw HD, Hollick JB, Parsons TJ, Clarke HRG, Gordon MP: Systemically wound-responsive genes in poplar trees encode proteins similar to sweet potato sporamins and legume Kunitz trypsin inhibitors. Plant Mol Biol 14: 51-59 (1989).
    • (1989) Plant Mol Biol , vol.14 , pp. 51-59
    • Bradshaw, H.D.1    Hollick, J.B.2    Parsons, T.J.3    Clarke, H.R.G.4    Gordon, M.P.5
  • 6
    • 0021765894 scopus 로고
    • Isolation and characterization of a wound-induced trypsin inhibitor from alfalfa leaves
    • Brown WE, Ryan CA: Isolation and characterization of a wound-induced trypsin inhibitor from alfalfa leaves. Biochemistry 23: 3418-3422 (1984).
    • (1984) Biochemistry , vol.23 , pp. 3418-3422
    • Brown, W.E.1    Ryan, C.A.2
  • 7
    • 0017153535 scopus 로고
    • Proteinase inhibitor II from potatoes: Isolation and characterization of its promoter components
    • Bryant J, Green TR, Gurusaddaiah S, Ryan CA: Proteinase inhibitor II from potatoes: isolation and characterization of its promoter components. Biochemistry 15: 3418-3424 (1976).
    • (1976) Biochemistry , vol.15 , pp. 3418-3424
    • Bryant, J.1    Green, T.R.2    Gurusaddaiah, S.3    Ryan, C.A.4
  • 8
    • 51249169259 scopus 로고
    • A simple and efficient method for isolating RNA from pine trees
    • Chang, Puryear, Cairney: A simple and efficient method for isolating RNA from pine trees. Plant Mol Biol Rep II (2): 117-121 (1993).
    • (1993) Plant Mol Biol Rep , vol.2 , Issue.2 , pp. 117-121
    • Chang, P.C.1
  • 9
    • 11944254202 scopus 로고
    • Interplant communication: Airborne methyl jasmonate induced synthesis of proteinase inhibitors in plant leaves
    • Farmer EE, Ryan CA: Interplant communication: airborne methyl jasmonate induced synthesis of proteinase inhibitors in plant leaves. Proc Natl Acad Sci USA 87: 7713-7716 (1990).
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7713-7716
    • Farmer, E.E.1    Ryan, C.A.2
  • 10
    • 0027212498 scopus 로고
    • Solubilization and purification of enzymatically active Glutathione S-Transferase (pGEX) fusion proteins
    • Frangioni JV, Neel BG: Solubilization and purification of enzymatically active Glutathione S-Transferase (pGEX) fusion proteins. Analytical Biochemistry 210: 179-187 (1993).
    • (1993) Analytical Biochemistry , vol.210 , pp. 179-187
    • Frangioni, J.V.1    Neel, B.G.2
  • 11
    • 0002681086 scopus 로고
    • Posttranscriptional regulation of gene expression in plants
    • Gallie D: Posttranscriptional regulation of gene expression in plants. Annu Rev Physiol Plant Mol Biol 44: 77-105 (1993).
    • (1993) Annu Rev Physiol Plant Mol Biol , vol.44 , pp. 77-105
    • Gallie, D.1
  • 13
    • 0025478627 scopus 로고
    • Isolation and characterization of a proteinaceous inhibitor of microbial proteinases induced during the hypersensitive reaction of tobacco to tobacco mosaic virus
    • Geoffroy P, Legrand M, Fritig B: Isolation and characterization of a proteinaceous inhibitor of microbial proteinases induced during the hypersensitive reaction of tobacco to tobacco mosaic virus. Molecular Plant-Microbe Interactions vol 3 No 5: 327-333 (1990).
    • (1990) Molecular Plant-Microbe Interactions , vol.3 , Issue.5 , pp. 327-333
    • Geoffroy, P.1    Legrand, M.2    Fritig, B.3
  • 14
    • 0001068883 scopus 로고
    • Wound-induced proteinase inhibitor in plant leaves: A possible defense mechanism against insects
    • Green RT, Ryan CA: Wound-induced proteinase inhibitor in plant leaves: a possible defense mechanism against insects. Science 175: 776-777 (1972).
    • (1972) Science , vol.175 , pp. 776-777
    • Green, R.T.1    Ryan, C.A.2
  • 15
    • 84982517944 scopus 로고
    • Genetics of field resistance to Melampsora in Salix viminalis
    • Gullberg U, Ryttman H: Genetics of field resistance to Melampsora in Salix viminalis. European J Forest Pathol 23 (2): 75-84 (1993).
    • (1993) European J Forest Pathol , vol.23 , Issue.2 , pp. 75-84
    • Gullberg, U.1    Ryttman, H.2
  • 16
    • 0001157197 scopus 로고
    • Genes encoding for the major tuberous root protein of sweet potato: Indentification of putative regulatory sequence in the 5' upstream region
    • Hattori T, Nakamura K: Genes encoding for the major tuberous root protein of sweet potato: Indentification of putative regulatory sequence in the 5' upstream region. Plant Mol Biol 11: 417-426 (1988).
    • (1988) Plant Mol Biol , vol.11 , pp. 417-426
    • Hattori, T.1    Nakamura, K.2
  • 17
    • 0024766915 scopus 로고
    • Structural relationship among the members of a multigene family coding for the sweet potato tuberous root storage protein
    • Hattori T, Yoshida N, Nakamura K: Structural relationship among the members of a multigene family coding for the sweet potato tuberous root storage protein. Plant Mol Biol 13: 563-572 (1989).
    • (1989) Plant Mol Biol , vol.13 , pp. 563-572
    • Hattori, T.1    Yoshida, N.2    Nakamura, K.3
  • 18
    • 0023188637 scopus 로고
    • Accelerated evolution in the reactive centre regions of serine protease inhibitors
    • Hill RE, Hastie ND: Accelerated evolution in the reactive centre regions of serine protease inhibitors. Nature 326: 96-99 (1987).
    • (1987) Nature , vol.326 , pp. 96-99
    • Hill, R.E.1    Hastie, N.D.2
  • 19
    • 0021238641 scopus 로고
    • Plasma protease inhibitors in mouse and man: Divergence within reactive centre regions
    • Hill RE, Shaw PH, Boyd PA, Baumann H, Hastie ND: Plasma protease inhibitors in mouse and man: divergence within reactive centre regions. Nature 311: 175-177 (1984).
    • (1984) Nature , vol.311 , pp. 175-177
    • Hill, R.E.1    Shaw, P.H.2    Boyd, P.A.3    Baumann, H.4    Hastie, N.D.5
  • 20
    • 0027638491 scopus 로고
    • A poplar tree proteinase inhibitor-like gene promoter is responsive to wounding in transgenic tobacco
    • Hollick JB, Gordon MP: A poplar tree proteinase inhibitor-like gene promoter is responsive to wounding in transgenic tobacco. Plant Mol Biol 22: 561-572 (1993).
    • (1993) Plant Mol Biol , vol.22 , pp. 561-572
    • Hollick, J.B.1    Gordon, M.P.2
  • 21
    • 0026778189 scopus 로고
    • Nucleotide sequence of cDNA for Acacia confusa trypsin inhibitor and implication of post-translation processing
    • Hung CH, Lee MC, Lin JY: Nucleotide sequence of cDNA for Acacia confusa trypsin inhibitor and implication of post-translation processing. Biochem Biophys Res Commun 184: 1524-1528 (1992).
    • (1992) Biochem Biophys Res Commun , vol.184 , pp. 1524-1528
    • Hung, C.H.1    Lee, M.C.2    Lin, J.Y.3
  • 22
    • 0024755662 scopus 로고
    • Kunitz trypsin inhibitor genes are differentially expressed during the soybean life cycle and in transformed tobacco plants
    • Jofuku KD, Goldberg RB: Kunitz trypsin inhibitor genes are differentially expressed during the soybean life cycle and in transformed tobacco plants. Plant Cell 1: 1079-1093 (1989).
    • (1989) Plant Cell , vol.1 , pp. 1079-1093
    • Jofuku, K.D.1    Goldberg, R.B.2
  • 23
    • 0023568135 scopus 로고
    • The primary structure of the inhibitor of tissue plasminogen activator found in the seeds of Erythrina caffra
    • Joubert FJ, Dowdle EBD: The primary structure of the inhibitor of tissue plasminogen activator found in the seeds of Erythrina caffra. Thromb Haemost 57: 356-360 (1987).
    • (1987) Thromb Haemost , vol.57 , pp. 356-360
    • Joubert, F.J.1    Dowdle, E.B.D.2
  • 24
    • 0002704134 scopus 로고
    • Auxin levels regulate the expression of a wound-inducible proteinase inhibitor II-chloramphenicol acetyl transferase gene fusion in vitro and in vivo
    • Kernan A, Thornburg RW: Auxin levels regulate the expression of a wound-inducible proteinase inhibitor II-chloramphenicol acetyl transferase gene fusion in vitro and in vivo. Plant Physiol 91: 73-78 (1989).
    • (1989) Plant Physiol , vol.91 , pp. 73-78
    • Kernan, A.1    Thornburg, R.W.2
  • 25
    • 0027349149 scopus 로고
    • Amino acid sequence of chymotrypsin inhibitor ECI from seeds of Erythrina variegata (Linn.) var. Orientalis
    • Kimura M, Kouzuma Y, Yamasaki N: Amino acid sequence of chymotrypsin inhibitor ECI from seeds of Erythrina variegata (Linn.) var. Orientalis. Biosci Biotechnol Biochem 57: 102-106 (1993).
    • (1993) Biosci Biotechnol Biochem , vol.57 , pp. 102-106
    • Kimura, M.1    Kouzuma, Y.2    Yamasaki, N.3
  • 26
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolitte RF: A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105-132 (1982).
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolitte, R.F.2
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227: 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski Jr M, Kato I: Protein inhibitors of proteinases. Annu Rev Biochem 49: 593-626 (1980).
    • (1980) Annu Rev Biochem , vol.49 , pp. 593-626
    • Laskowski Jr., M.1    Kato, I.2
  • 29
    • 0021919480 scopus 로고
    • Rapid and sensitive protein similarity searches
    • Lipman DJ, Pearson WR: Rapid and sensitive protein similarity searches. Science 227: 1435-1441 (1985).
    • (1985) Science , vol.227 , pp. 1435-1441
    • Lipman, D.J.1    Pearson, W.R.2
  • 31
    • 0024972959 scopus 로고
    • Primary structure of cathepsin D inhibitor from potatoes and its structure relationship to soybean trypsin inhibitor family
    • Mares M, Meloun B, Palvik M, Kostka V, Baudys M: Primary structure of cathepsin D inhibitor from potatoes and its structure relationship to soybean trypsin inhibitor family. Febs Lett 251: 94-98 (1989).
    • (1989) Febs Lett , vol.251 , pp. 94-98
    • Mares, M.1    Meloun, B.2    Palvik, M.3    Kostka, V.4    Baudys, M.5
  • 32
    • 0027134032 scopus 로고
    • Protein targetting to the vacuole in plant cells
    • Nakamura K, Matsuoka K: Protein targetting to the vacuole in plant cells. Plant Physiol 101: 1-5 (1993).
    • (1993) Plant Physiol , vol.101 , pp. 1-5
    • Nakamura, K.1    Matsuoka, K.2
  • 33
    • 0026743915 scopus 로고
    • The amino acid sequence of a 20 kDa bifunctional subtilisin/alpha-amylase inhibitor from bran of rice (Oryza sativa L:) seeds
    • Ohtsubo KI, Richardson M: The amino acid sequence of a 20 kDa bifunctional subtilisin/alpha-amylase inhibitor from bran of rice (Oryza sativa L:) seeds. Febs Lett 309: 68-72 (1992).
    • (1992) Febs Lett , vol.309 , pp. 68-72
    • Ohtsubo, K.I.1    Richardson, M.2
  • 34
    • 0026166366 scopus 로고
    • Differential expression of tomato proteinase inhibitor I and II genes during bacterial pathogen invasion and wounding
    • Pautot V, Holzer FM, Walling LL: Differential expression of tomato proteinase inhibitor I and II genes during bacterial pathogen invasion and wounding. Mol. Plant Microbe Inter 4: 284-292 (1991).
    • (1991) Mol. Plant Microbe Inter , vol.4 , pp. 284-292
    • Pautot, V.1    Holzer, F.M.2    Walling, L.L.3
  • 35
    • 0025886794 scopus 로고
    • A polypeptide from tomato leaves induces wound-inducible proteinase inhibitor proteins
    • Pearce G, Strydom D, Johnson S, Ryan CA: A polypeptide from tomato leaves induces wound-inducible proteinase inhibitor proteins. Science 253: 895-898 (1991).
    • (1991) Science , vol.253 , pp. 895-898
    • Pearce, G.1    Strydom, D.2    Johnson, S.3    Ryan, C.A.4
  • 36
    • 0024820609 scopus 로고
    • Abscisic acid is involved in the wound-induced expression of the proteinase inhibitor II gene in potato and tomato
    • Pena-Cortes H, Sanchez-Serrano JJ, Mertens R, Willmitzer L, Prat S: Abscisic acid is involved in the wound-induced expression of the proteinase inhibitor II gene in potato and tomato. Proc Natl Acad Sci USA 86: 9851-9855 (1989).
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9851-9855
    • Pena-Cortes, H.1    Sanchez-Serrano, J.J.2    Mertens, R.3    Willmitzer, L.4    Prat, S.5
  • 37
    • 0020096073 scopus 로고
    • Proteinase inhibitors I and II from leaves of wounded tomato plants: Purification and properties
    • Plunkett G, Senear DF, Zuroske G, Ryan CA: Proteinase inhibitors I and II from leaves of wounded tomato plants: purification and properties. Arch Biochem Biophys 213: 463-472 (1982).
    • (1982) Arch Biochem Biophys , vol.213 , pp. 463-472
    • Plunkett, G.1    Senear, D.F.2    Zuroske, G.3    Ryan, C.A.4
  • 38
    • 0003315576 scopus 로고
    • Nucleic acid hybridizations with positive charge-modified nylon membrane
    • Reed KC: Nucleic acid hybridizations with positive charge-modified nylon membrane. Methods in Gene Technology Vol 1: 127-160 (1991).
    • (1991) Methods in Gene Technology , vol.1 , pp. 127-160
    • Reed, K.C.1
  • 40
    • 84969779596 scopus 로고
    • Induction of proteinase inhibitors in tobacco cell suspension culture by elicitors of Phytophthora parasitica var. nicotianae
    • Rickauer M, Fournier J, Esquerré-Tougayé M-T: Induction of proteinase inhibitors in tobacco cell suspension culture by elicitors of Phytophthora parasitica var. nicotianae. Plant Physiol 90: 1065-1070 (1989).
    • (1989) Plant Physiol , vol.90 , pp. 1065-1070
    • Rickauer, M.1    Fournier, J.2    Esquerré-Tougayé, M.-T.3
  • 41
    • 0028065553 scopus 로고
    • Systematic Acquired Resistance
    • Ryals J, Uknes S, Ward E: Systematic Acquired Resistance. Plant Physiol 104: 1109-1112 (1994).
    • (1994) Plant Physiol , vol.104 , pp. 1109-1112
    • Ryals, J.1    Uknes, S.2    Ward, E.3
  • 44
    • 0037701465 scopus 로고
    • Genetic differences in wound-induced ethylene production among different clones of Salix viminalis L. Silvae
    • Saarikoski P, von Arnold S, Clapham D, Gullberg U: Genetic differences in wound-induced ethylene production among different clones of Salix viminalis L. Silvae Genetica 42: 121-126 (1993).
    • (1993) Genetica , vol.42 , pp. 121-126
    • Saarikoski, P.1    Von Arnold, S.2    Clapham, D.3    Gullberg, U.4
  • 45
    • 0001188372 scopus 로고
    • Evidence for the presence of proteinase inhibitor I in vacuolar protein bodies of plant cells
    • Shumway LK, Yang VV, Ryan CA: Evidence for the presence of proteinase inhibitor I in vacuolar protein bodies of plant cells. Planta 129: 161-165 (1976).
    • (1976) Planta , vol.129 , pp. 161-165
    • Shumway, L.K.1    Yang, V.V.2    Ryan, C.A.3
  • 46
    • 0001101460 scopus 로고
    • Discontinuous genetic variation in resistance of Salix viminalis L to a gall-midge attack
    • Strong D, Larsson S, Gullberg U: Discontinuous genetic variation in resistance of Salix viminalis L to a gall-midge attack. Evolution 47 (1): 291-300 (1993).
    • (1993) Evolution , vol.47 , Issue.1 , pp. 291-300
    • Strong, D.1    Larsson, S.2    Gullberg, U.3
  • 47
    • 0026166258 scopus 로고
    • Nucleic acid sequence of a 21 kDa cocoa seed protein with homology to the soybean trypsin inhibitor (Kunitz) family of protease inhibitors
    • Tai H, Mchenry L, Fritz PJ, Furtek DB: Nucleic acid sequence of a 21 kDa cocoa seed protein with homology to the soybean trypsin inhibitor (Kunitz) family of protease inhibitors. Plant Mol Biol 16: 913-915 (1991).
    • (1991) Plant Mol Biol , vol.16 , pp. 913-915
    • Tai, H.1    Mchenry, L.2    Fritz, P.J.3    Furtek, D.B.4
  • 48
    • 0024533487 scopus 로고
    • Complete amino acid sequence and structure characterization of the taste-modifying protein, miraculin
    • Theerasilp S, Hitotsuya H, Nakajo S, Nakaja K, Nakamura Y, Kurihara Y: Complete amino acid sequence and structure characterization of the taste-modifying protein, miraculin. J Biol Chem 264: 6655-6659 (1989).
    • (1989) J Biol Chem , vol.264 , pp. 6655-6659
    • Theerasilp, S.1    Hitotsuya, H.2    Nakajo, S.3    Nakaja, K.4    Nakamura, Y.5    Kurihara, Y.6
  • 49
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • Von Heijne G: A new method for predicting signal sequence cleavage sites. Nucleic Acids 14: 4683-4690 (1986).
    • (1986) Nucleic Acids , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 50
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal sequence cleavage site
    • Von Heijne G: Patterns of amino acids near signal sequence cleavage site. Eur J Biochem 133: 17-21 (1983).
    • (1983) Eur J Biochem , vol.133 , pp. 17-21
    • Von Heijne, G.1
  • 52
    • 0020819885 scopus 로고
    • Amino acid sequences of two trypsin inhibitors from winged bean seeds (Psophocarpus tetragonolobus (L) DC)
    • Yamanioto M, Kara S, Ikenaka T: Amino acid sequences of two trypsin inhibitors from winged bean seeds (Psophocarpus tetragonolobus (L) DC). J Biochem 94: 849-863 (1983).
    • (1983) J Biochem , vol.94 , pp. 849-863
    • Yamanioto, M.1    Kara, S.2    Ikenaka, T.3
  • 53
    • 45949130041 scopus 로고
    • The amino acid sequence and reactive (inhibitory) site of the major trypsin isoinhibitor (DE5) isolated from seeds of the Brazilian Carolina tree (Adenanthera pavonina L.)
    • Yarwood A: The amino acid sequence and reactive (inhibitory) site of the major trypsin isoinhibitor (DE5) isolated from seeds of the Brazilian Carolina tree (Adenanthera pavonina L.): Biochim Biophys Acta 872: 134-140 (1986).
    • (1986) Biochim Biophys Acta , vol.872 , pp. 134-140
    • Yarwood, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.