메뉴 건너뛰기




Volumn 68, Issue 4-6, 2006, Pages 138-148

Identification and characterization of potato protease inhibitors able to inhibit pathogenicity and growth of Botrytis cinerea

Author keywords

Anti fungal; Bemisia tabaci; Botrytis cinerea; Kunitz type inhibitor; Proteinase inhibitor 1; Proteinase inhibitors; Solanum tuberosum

Indexed keywords

BEMISIA TABACI; BOTRYOTINIA FUCKELIANA; FUNGI; HEXAPODA; NICOTIANA TABACUM; SOLANUM TUBEROSUM;

EID: 33847083461     PISSN: 08855765     EISSN: 10961178     Source Type: Journal    
DOI: 10.1016/j.pmpp.2006.09.004     Document Type: Article
Times cited : (38)

References (49)
  • 1
    • 0030887368 scopus 로고    scopus 로고
    • Fungal pathogens secrete an inhibitor protein that distinguishes isoforms of plant pathogenesis related endo-β-1,3-glucanases
    • Kyung Sik H., Sheng Cheng W., Darvill A., and Albersheim P. Fungal pathogens secrete an inhibitor protein that distinguishes isoforms of plant pathogenesis related endo-β-1,3-glucanases. Plant J 11 (1997) 169-179
    • (1997) Plant J , vol.11 , pp. 169-179
    • Kyung Sik, H.1    Sheng Cheng, W.2    Darvill, A.3    Albersheim, P.4
  • 4
    • 28044470978 scopus 로고    scopus 로고
    • Evolutionary mechanisms acting on proteinase inhibitor variability
    • Christeller J.T. Evolutionary mechanisms acting on proteinase inhibitor variability. FEBS J 272 (2005) 5710-5722
    • (2005) FEBS J , vol.272 , pp. 5710-5722
    • Christeller, J.T.1
  • 5
    • 1642464622 scopus 로고    scopus 로고
    • Evolutionary families of peptidase inhibitors
    • Rawlings N.D., Tolle D.P., and Barrett A.J. Evolutionary families of peptidase inhibitors. Biochem J 378 (2004) 705-716
    • (2004) Biochem J , vol.378 , pp. 705-716
    • Rawlings, N.D.1    Tolle, D.P.2    Barrett, A.J.3
  • 6
    • 0035823595 scopus 로고    scopus 로고
    • The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
    • Silverman G.A., Bird P.I., Carrell R.W., Church F.C., Coughlin P.B., Gettins P.G., et al. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J Biol Chem 276 (2001) 33293-33296
    • (2001) J Biol Chem , vol.276 , pp. 33293-33296
    • Silverman, G.A.1    Bird, P.I.2    Carrell, R.W.3    Church, F.C.4    Coughlin, P.B.5    Gettins, P.G.6
  • 7
    • 33847037177 scopus 로고    scopus 로고
    • The possible role of PR proteins in multigenic and induced systemic resistance
    • Tuzun S., and Bent E. (Eds), Springer, New York
    • Tuzun S., and Somanchi A. The possible role of PR proteins in multigenic and induced systemic resistance. In: Tuzun S., and Bent E. (Eds). Multigenic and induced systemic resistance in plants (2006), Springer, New York 112-142
    • (2006) Multigenic and induced systemic resistance in plants , pp. 112-142
    • Tuzun, S.1    Somanchi, A.2
  • 8
    • 0033179482 scopus 로고    scopus 로고
    • The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins
    • Van Loon L.C., and Van Strien E.A. The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins. Physiol Mol Plant Pathol 55 (1999) 85-97
    • (1999) Physiol Mol Plant Pathol , vol.55 , pp. 85-97
    • Van Loon, L.C.1    Van Strien, E.A.2
  • 10
    • 27944443661 scopus 로고    scopus 로고
    • Characteristics of plant proteinase inhibitors and their applications in combating phytophagous insects
    • Fan S.G., and Wu G.J. Characteristics of plant proteinase inhibitors and their applications in combating phytophagous insects. Bot Bull Acad Sin 46 (2005) 273-292
    • (2005) Bot Bull Acad Sin , vol.46 , pp. 273-292
    • Fan, S.G.1    Wu, G.J.2
  • 13
    • 0038057913 scopus 로고    scopus 로고
    • Sporamin-mediated resistance to beet cyst nematodes (Heterodera schachtii Schm.) is dependent on trypsin inhibitory activity in sugar beet (Beta vulgaris L.) hairy roots
    • Cai D., Thurau T., Tian Y., Lange T., Yeh K., and Jung C. Sporamin-mediated resistance to beet cyst nematodes (Heterodera schachtii Schm.) is dependent on trypsin inhibitory activity in sugar beet (Beta vulgaris L.) hairy roots. Plant Mol Biol 51 (2003) 839-849
    • (2003) Plant Mol Biol , vol.51 , pp. 839-849
    • Cai, D.1    Thurau, T.2    Tian, Y.3    Lange, T.4    Yeh, K.5    Jung, C.6
  • 14
    • 0032787406 scopus 로고    scopus 로고
    • The use of cysteine proteinase inhibitors to engineer resistance against potyviruses in transgenic tobacco plants
    • Gutierrez-Campos R., Torres-Acosta J.A., Saucedo-Arias L.J., and Gomez-Lim M.A. The use of cysteine proteinase inhibitors to engineer resistance against potyviruses in transgenic tobacco plants. Nat Biotechnol 17 (1999) 1223-1226
    • (1999) Nat Biotechnol , vol.17 , pp. 1223-1226
    • Gutierrez-Campos, R.1    Torres-Acosta, J.A.2    Saucedo-Arias, L.J.3    Gomez-Lim, M.A.4
  • 15
    • 0026598850 scopus 로고
    • Isolation and characterization of a 22 kDa protein with antifungal properties from maize seeds
    • Huynh Q.K., Borgmeyer J.R., and Zobel J.F. Isolation and characterization of a 22 kDa protein with antifungal properties from maize seeds. Biochem Biophys Res Commun 182 (1992) 1-5
    • (1992) Biochem Biophys Res Commun , vol.182 , pp. 1-5
    • Huynh, Q.K.1    Borgmeyer, J.R.2    Zobel, J.F.3
  • 16
    • 0027132885 scopus 로고
    • Synergistic enhancement of the antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and by barley trypsin inhibitors
    • Terras F.R., Schoofs H.M.E., Thevissen K., Osborn R.W., Vanderleyden J., Cammue B.P.A., et al. Synergistic enhancement of the antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and by barley trypsin inhibitors. Plant Physiol 103 (1993) 1311-1319
    • (1993) Plant Physiol , vol.103 , pp. 1311-1319
    • Terras, F.R.1    Schoofs, H.M.E.2    Thevissen, K.3    Osborn, R.W.4    Vanderleyden, J.5    Cammue, B.P.A.6
  • 17
    • 0041402695 scopus 로고    scopus 로고
    • Functional comparison of homologous members of three groups of Kunitz-type enzyme inhibitors from potato tubers (Solanum tuberosum L.)
    • Heibges A., Salamini F., and Gebhardt C. Functional comparison of homologous members of three groups of Kunitz-type enzyme inhibitors from potato tubers (Solanum tuberosum L.). Mol Genet Genomics 269 (2003) 535-541
    • (2003) Mol Genet Genomics , vol.269 , pp. 535-541
    • Heibges, A.1    Salamini, F.2    Gebhardt, C.3
  • 19
    • 27744440981 scopus 로고    scopus 로고
    • Expression of the maize proteinase inhibitor (mpi) gene in rice plants enhances resistance against the striped stem borer (Chilo suppressalis): effects on larval growth and insect gut proteinases
    • Vila L., Quilis J., Meynard D., Breitler J.C., Marfà V., Murillo I., et al. Expression of the maize proteinase inhibitor (mpi) gene in rice plants enhances resistance against the striped stem borer (Chilo suppressalis): effects on larval growth and insect gut proteinases. Plant Biotechnol J 3 (2005) 187-202
    • (2005) Plant Biotechnol J , vol.3 , pp. 187-202
    • Vila, L.1    Quilis, J.2    Meynard, D.3    Breitler, J.C.4    Marfà, V.5    Murillo, I.6
  • 20
    • 5344259633 scopus 로고    scopus 로고
    • Protein proteinase inhibitor genes in combat against insects, pests, and pathogens: natural and engineered phytoprotection
    • Haq S.K., Atif S.M., and Khan R.H. Protein proteinase inhibitor genes in combat against insects, pests, and pathogens: natural and engineered phytoprotection. Arch Biochem Biophys 431 (2004) 145-159
    • (2004) Arch Biochem Biophys , vol.431 , pp. 145-159
    • Haq, S.K.1    Atif, S.M.2    Khan, R.H.3
  • 22
    • 0001503501 scopus 로고
    • Molecular characterization of a wound inducible inhibitor I gene from potato and the processing of its messenger RNA and protein
    • Cleveland T.E., Thornburg R.W., and Ryan C.A. Molecular characterization of a wound inducible inhibitor I gene from potato and the processing of its messenger RNA and protein. Plant Mol Biol 8 (1987) 199-207
    • (1987) Plant Mol Biol , vol.8 , pp. 199-207
    • Cleveland, T.E.1    Thornburg, R.W.2    Ryan, C.A.3
  • 23
    • 0022796012 scopus 로고
    • Molecular characterization and phylogenetic studies of a wound-inducible proteinase inhibitor I gene in Lycopersicon species
    • Lee J.S., Brown W.E., Graham J.S., Pearce G., Fox E.A., Dreher T.W., et al. Molecular characterization and phylogenetic studies of a wound-inducible proteinase inhibitor I gene in Lycopersicon species. Proc Natl Acad Sci USA 83 (1986) 7277-7281
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 7277-7281
    • Lee, J.S.1    Brown, W.E.2    Graham, J.S.3    Pearce, G.4    Fox, E.A.5    Dreher, T.W.6
  • 24
    • 0028853169 scopus 로고
    • Inhibition of larval growth by patatin, the lipid acylhydrolase from potato tubers
    • Strickland J.A., Orr G.L., and Walsh T.A. Inhibition of larval growth by patatin, the lipid acylhydrolase from potato tubers. Plant Physiol 109 (1995) 667-674
    • (1995) Plant Physiol , vol.109 , pp. 667-674
    • Strickland, J.A.1    Orr, G.L.2    Walsh, T.A.3
  • 25
    • 0041402696 scopus 로고    scopus 로고
    • Structural diversity and organization of three gene families for Kunitz-type enzyme inhibitors from potato tubers (Solanum tuberosum L.)
    • Heibges A., Glaczinski H., Ballvora A., Salamini F., and Gebhardt C. Structural diversity and organization of three gene families for Kunitz-type enzyme inhibitors from potato tubers (Solanum tuberosum L.). Mol Genet Genomics 269 (2003) 526-534
    • (2003) Mol Genet Genomics , vol.269 , pp. 526-534
    • Heibges, A.1    Glaczinski, H.2    Ballvora, A.3    Salamini, F.4    Gebhardt, C.5
  • 26
    • 0000544299 scopus 로고
    • A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels
    • Oakley B.R., Kirsch D.R., and Morris N.R. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal Biochem 105 (1980) 361-363
    • (1980) Anal Biochem , vol.105 , pp. 361-363
    • Oakley, B.R.1    Kirsch, D.R.2    Morris, N.R.3
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 0001455051 scopus 로고
    • Increased proteinase inhibitor activity in response to infection of resistant tomato plant by Phytophthora infestans
    • Peng J.H., and Black L.L. Increased proteinase inhibitor activity in response to infection of resistant tomato plant by Phytophthora infestans. Phytopathology 66 (1976) 958-963
    • (1976) Phytopathology , vol.66 , pp. 958-963
    • Peng, J.H.1    Black, L.L.2
  • 30
    • 0028055658 scopus 로고
    • Purification, characterization and synergistic activity of a glucan 1,3-β-glucosidase and an N-acetyl-β-glucosaminidase from Trichoderma harzianum
    • Lorito M., Hayes C.K., Di Pietro A., Woo S.L., and Harman G.E. Purification, characterization and synergistic activity of a glucan 1,3-β-glucosidase and an N-acetyl-β-glucosaminidase from Trichoderma harzianum. Phytopathology 84 (1994) 398-405
    • (1994) Phytopathology , vol.84 , pp. 398-405
    • Lorito, M.1    Hayes, C.K.2    Di Pietro, A.3    Woo, S.L.4    Harman, G.E.5
  • 32
    • 0002594984 scopus 로고
    • A rapid DNA isolation procedure from small quantities of fresh leaf tissues
    • Doyle J.J., and Doyle J.L. A rapid DNA isolation procedure from small quantities of fresh leaf tissues. Phytochem Bull 19 (1987) 11-15
    • (1987) Phytochem Bull , vol.19 , pp. 11-15
    • Doyle, J.J.1    Doyle, J.L.2
  • 33
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., and Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162 (1987) 156-159
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 34
    • 0029791403 scopus 로고    scopus 로고
    • Splice site prediction in Arabidopsis thaliana pre-mRNA by combining local and global sequence information
    • Hebsgaard S.M., Korning P.G., Tolstrup N., Engelbrecht J., Rouze P., and Brunak S. Splice site prediction in Arabidopsis thaliana pre-mRNA by combining local and global sequence information. Nucleic Acids Res 24 (1996) 3439-3452
    • (1996) Nucleic Acids Res , vol.24 , pp. 3439-3452
    • Hebsgaard, S.M.1    Korning, P.G.2    Tolstrup, N.3    Engelbrecht, J.4    Rouze, P.5    Brunak, S.6
  • 35
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S., Tamura K., and Nei M. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Briefings Bioinformatics 5 (2004) 150-163
    • (2004) Briefings Bioinformatics , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 36
    • 0002514061 scopus 로고
    • Two Kunitz-type proteinase inhibitors from potato tubers
    • Walsh T.A., and Twichell W.P. Two Kunitz-type proteinase inhibitors from potato tubers. Plant Physiol 97 (1991) 15-18
    • (1991) Plant Physiol , vol.97 , pp. 15-18
    • Walsh, T.A.1    Twichell, W.P.2
  • 37
    • 3242708870 scopus 로고    scopus 로고
    • Characterization of a proteinase inhibitor from Brachypodium distachyon suggests the conservation of defence signalling pathways between dicotyledonous plants and grasses
    • Mur L.A.J., Xu R., Casson S.A., Stoddart W.M., Routledge A.P.M., and Draper J. Characterization of a proteinase inhibitor from Brachypodium distachyon suggests the conservation of defence signalling pathways between dicotyledonous plants and grasses. Mol Plant Pathol 5 (2004) 267-280
    • (2004) Mol Plant Pathol , vol.5 , pp. 267-280
    • Mur, L.A.J.1    Xu, R.2    Casson, S.A.3    Stoddart, W.M.4    Routledge, A.P.M.5    Draper, J.6
  • 38
    • 0029053258 scopus 로고
    • A basic serine protease from Paecilomyces lilacinus with biological activity against Meloidogyne hapla
    • Bonants P.J., Fitters P.F., Thijs H., den Belder E., Waalwijk C., and Henfling J.W. A basic serine protease from Paecilomyces lilacinus with biological activity against Meloidogyne hapla. Microbiology 141 (1995) 775-784
    • (1995) Microbiology , vol.141 , pp. 775-784
    • Bonants, P.J.1    Fitters, P.F.2    Thijs, H.3    den Belder, E.4    Waalwijk, C.5    Henfling, J.W.6
  • 40
    • 0028141988 scopus 로고
    • Isoforms of the cuticle-degrading Pr1 proteinase and production of a metalloproteinase by Metarhizium anisopliae
    • St Leger R.J., Bidochka M.J., and Roberts D.W. Isoforms of the cuticle-degrading Pr1 proteinase and production of a metalloproteinase by Metarhizium anisopliae. Arch Biochem Biophys 313 (1994) 1-7
    • (1994) Arch Biochem Biophys , vol.313 , pp. 1-7
    • St Leger, R.J.1    Bidochka, M.J.2    Roberts, D.W.3
  • 42
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M.J., and Kato I. Protein inhibitors of proteinases. Annu Rev Biochem 49 (1980) 593-626
    • (1980) Annu Rev Biochem , vol.49 , pp. 593-626
    • Laskowski, M.J.1    Kato, I.2
  • 43
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode W., and Huber R. Natural protein proteinase inhibitors and their interaction with proteinases. Eur J Biochem 204 (1992) 433-451
    • (1992) Eur J Biochem , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 44
    • 0027236764 scopus 로고
    • cDNA cloning and gene expression analysis of the microbial proteinase inhibitor of tobacco
    • Heitz T., Geoffrey P., Stinti A., Fritig B., and Legrand M. cDNA cloning and gene expression analysis of the microbial proteinase inhibitor of tobacco. J Biol Chem 268 (1993) 16987-16992
    • (1993) J Biol Chem , vol.268 , pp. 16987-16992
    • Heitz, T.1    Geoffrey, P.2    Stinti, A.3    Fritig, B.4    Legrand, M.5
  • 45
    • 23944503272 scopus 로고    scopus 로고
    • Single mutation at P1 of a chymotrypsin inhibitor changes it to a trypsin inhibitor: X-ray structural (2.15 A) and biochemical basis
    • Khamrui S., Dasgupta J., Dattagupta J.K., and Sen U. Single mutation at P1 of a chymotrypsin inhibitor changes it to a trypsin inhibitor: X-ray structural (2.15 A) and biochemical basis. Biochim Biophys Acta 1752 (2005) 65-72
    • (2005) Biochim Biophys Acta , vol.1752 , pp. 65-72
    • Khamrui, S.1    Dasgupta, J.2    Dattagupta, J.K.3    Sen, U.4
  • 46
    • 0015576315 scopus 로고
    • Studies on soybean trypsin inhibitors. 3. Amino acid sequences of the carboxyl-terminal region and the complete amino acid sequence of soybean trypsin inhibitor (Kunitz)
    • Koide T., and Ikenaka T. Studies on soybean trypsin inhibitors. 3. Amino acid sequences of the carboxyl-terminal region and the complete amino acid sequence of soybean trypsin inhibitor (Kunitz). Eur J Biochem 32 (1973) 417-431
    • (1973) Eur J Biochem , vol.32 , pp. 417-431
    • Koide, T.1    Ikenaka, T.2
  • 47
    • 0003815183 scopus 로고
    • Purification and characterization of the 22-kilodalton potato tuber proteins
    • Suh S.G., Peterson J.E., Stiekema W.J., and Hannapel D.J. Purification and characterization of the 22-kilodalton potato tuber proteins. Plant Physiol 94 (1990) 40-45
    • (1990) Plant Physiol , vol.94 , pp. 40-45
    • Suh, S.G.1    Peterson, J.E.2    Stiekema, W.J.3    Hannapel, D.J.4
  • 49
    • 0024804111 scopus 로고
    • Expression of proteinase inhibitors I and II in transgenic tobacco plants: effects on natural defense against Manduca sexta larvae
    • Johnson R., Narvaez J., An G., and Ryan C. Expression of proteinase inhibitors I and II in transgenic tobacco plants: effects on natural defense against Manduca sexta larvae. Proc Natl Acad Sci USA 86 (1989) 9871-9875
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9871-9875
    • Johnson, R.1    Narvaez, J.2    An, G.3    Ryan, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.