메뉴 건너뛰기




Volumn 580, Issue 3, 2006, Pages 948-954

One of the three proteinase inhibitor genes newly identified in the Brassica napus genome codes for an inhibitor of glutamyl endopeptidase

Author keywords

Germination; Glutamyl proteinase inhibitor; Proteinase inhibitor gene; Rapeseed

Indexed keywords

PROTEIN RTI 1; PROTEIN RTI 2; PROTEIN RTI 3; PROTEINASE INHIBITOR; RECOMBINANT PROTEIN; TRYPSIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 31444442624     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.01.022     Document Type: Article
Times cited : (8)

References (37)
  • 2
    • 0026552471 scopus 로고
    • Purification, inhibitory properties and amino acid sequence of a new serine proteinase inhibitor from white mustard (Sinapis alba L.) seeds
    • E. Menegatti, G. Tedeschi, S. Ronchi, F. Bortolotti, P. Ascenzi, R.M. Thomas, M. Bolognesi, and S. Palmieri Purification, inhibitory properties and amino acid sequence of a new serine proteinase inhibitor from white mustard (Sinapis alba L.) seeds FEBS Lett. 301 1992 10 14
    • (1992) FEBS Lett. , vol.301 , pp. 10-14
    • Menegatti, E.1    Tedeschi, G.2    Ronchi, S.3    Bortolotti, F.4    Ascenzi, P.5    Thomas, R.M.6    Bolognesi, M.7    Palmieri, S.8
  • 3
    • 0028219989 scopus 로고
    • Purification, inhibitory properties, amino acid sequence and identification of the reactive site of a new serine proteinase inhibitor from oil-rape (Brassica napus) seeds
    • F. Ceciliani, F. Bortolotti, E. Menegatti, S. Ronchi, P. Ascenzi, and S. Palmieri Purification, inhibitory properties, amino acid sequence and identification of the reactive site of a new serine proteinase inhibitor from oil-rape (Brassica napus) seeds FEBS Lett. 342 1994 221 224
    • (1994) FEBS Lett. , vol.342 , pp. 221-224
    • Ceciliani, F.1    Bortolotti, F.2    Menegatti, E.3    Ronchi, S.4    Ascenzi, P.5    Palmieri, S.6
  • 5
    • 0000051893 scopus 로고    scopus 로고
    • Opposite effects on Spodoptera littoralis larvae of low and high expression level of a trypsin proteinase inhibitor in transgenic plants
    • F. De Leo, M. Bonadé-Bottino, L.R. Ceci, R. Gallerani, and L. Jouanin Opposite effects on Spodoptera littoralis larvae of low and high expression level of a trypsin proteinase inhibitor in transgenic plants Plant Physiol. 118 1998 997 1004
    • (1998) Plant Physiol. , vol.118 , pp. 997-1004
    • De Leo, F.1    Bonadé-Bottino, M.2    Ceci, L.R.3    Gallerani, R.4    Jouanin, L.5
  • 7
    • 0033963158 scopus 로고    scopus 로고
    • Characterization of recombinant mustard trypsin inhibitor 2 (MTI2) expressed in Pichia pastoris
    • M. Volpicella, A. Schipper, M.A. Jongsma, N. Spoto, R. Gallerani, and L.R. Ceci Characterization of recombinant mustard trypsin inhibitor 2 (MTI2) expressed in Pichia pastoris FEBS Lett. 468 2000 137 141
    • (2000) FEBS Lett. , vol.468 , pp. 137-141
    • Volpicella, M.1    Schipper, A.2    Jongsma, M.A.3    Spoto, N.4    Gallerani, R.5    Ceci, L.R.6
  • 9
    • 0037327370 scopus 로고    scopus 로고
    • Selection by phage display of a variant mustard trypsin inhibitor toxic against aphids
    • L.R. Ceci, M. Volpicella, Y. Rahbé, R. Gallerani, J. Beekwilder, and M.A. Jongsma Selection by phage display of a variant mustard trypsin inhibitor toxic against aphids Plant J. 33 2003 557 566
    • (2003) Plant J. , vol.33 , pp. 557-566
    • Ceci, L.R.1    Volpicella, M.2    Rahbé, Y.3    Gallerani, R.4    Beekwilder, J.5    Jongsma, M.A.6
  • 10
  • 14
    • 0037428257 scopus 로고    scopus 로고
    • Protein minimization: Characterization of the synthetic cyclic dodecapeptide corresponding to the reactive site region of the oil rape trypsin inhibitor type-III
    • M. Trovato, E.C. Casavola, B. Maras, M.E. Schinina, P. Costantino, and P. Ascenzi Protein minimization: characterization of the synthetic cyclic dodecapeptide corresponding to the reactive site region of the oil rape trypsin inhibitor type-III Biochem. Biophys. Res. Commun. 302 2003 311 315
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 311-315
    • Trovato, M.1    Casavola, E.C.2    Maras, B.3    Schinina, M.E.4    Costantino, P.5    Ascenzi, P.6
  • 16
    • 0035034781 scopus 로고    scopus 로고
    • Analysis of mustard trypsin inhibitor-2 gene expression in response to developmental or environmental induction
    • F. De Leo, L.R. Ceci, L. Jouanin, and R. Gallerani Analysis of mustard trypsin inhibitor-2 gene expression in response to developmental or environmental induction Planta 212 2001 710 717
    • (2001) Planta , vol.212 , pp. 710-717
    • De Leo, F.1    Ceci, L.R.2    Jouanin, L.3    Gallerani, R.4
  • 18
    • 0028969475 scopus 로고
    • The gene coding for the mustard trypsin inhibitor-2 is discontinuous and wound-inducible
    • L.R. Ceci, N. Spoto, M. de Virgilio, and R. Gallerani The gene coding for the mustard trypsin inhibitor-2 is discontinuous and wound-inducible FEBS Lett. 364 1995 179 181
    • (1995) FEBS Lett. , vol.364 , pp. 179-181
    • Ceci, L.R.1    Spoto, N.2    De Virgilio, M.3    Gallerani, R.4
  • 20
    • 77049129946 scopus 로고
    • Pancreatic trypsin inhibitor. II. Reaction with trypsin
    • N.M. Green, and E. Work Pancreatic trypsin inhibitor. II. Reaction with trypsin Biochem. J. 54 1953 347 352
    • (1953) Biochem. J. , vol.54 , pp. 347-352
    • Green, N.M.1    Work, E.2
  • 21
    • 0034086003 scopus 로고    scopus 로고
    • Characterization of potato proteinase inhibitor II reactive site mutants
    • J. Beekwilder, B. Schipper, P. Bakker, D. Bosch, and M. Jongsma Characterization of potato proteinase inhibitor II reactive site mutants Eur. J. Biochem. 267 2000 1975 1984
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1975-1984
    • Beekwilder, J.1    Schipper, B.2    Bakker, P.3    Bosch, D.4    Jongsma, M.5
  • 22
    • 0027658084 scopus 로고
    • Characterization of the gene encoding the glutamic-acid-specific protease of Streptomyces griseus
    • S.S. Sidhu, G.B. Kalmar, and T.J. Borgford Characterization of the gene encoding the glutamic-acid-specific protease of Streptomyces griseus Biochem. Cell Biol. 71 1993 454 461
    • (1993) Biochem. Cell Biol. , vol.71 , pp. 454-461
    • Sidhu, S.S.1    Kalmar, G.B.2    Borgford, T.J.3
  • 23
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • J.D. Thompson, T.J. Gibson, F. Plewniak, F. Jeanmougin, and D.G. Higgins The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools Nucl. Acids Res. 25 1997 4876 4882
    • (1997) Nucl. Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 24
    • 0003437299 scopus 로고    scopus 로고
    • Distributed by the author. Department of Genome Sciences, University of Washington, Seattle.
    • Felsenstein, J. (2004) PHYLIP (Phylogeny Inference Package) version 3.6. Distributed by the author. Department of Genome Sciences, University of Washington, Seattle. Available from: 〈http://evolution.genetics.washington. edu/phylip.html〉.
    • (2004) PHYLIP (Phylogeny Inference Package) Version 3.6
    • Felsenstein, J.1
  • 25
    • 0000732090 scopus 로고
    • Evolution of protein molecules
    • H.N. Munro Academic Press New York, NY
    • T.H. Jukes, and C.R. Cantor Evolution of protein molecules H.N. Munro Mammalian Protein Metabolism 1969 Academic Press New York, NY 21 132
    • (1969) Mammalian Protein Metabolism , pp. 21-132
    • Jukes, T.H.1    Cantor, C.R.2
  • 26
    • 0029853148 scopus 로고    scopus 로고
    • WWW-Query: An on-line retrieval system for biological sequence banks
    • G. Perrière, and M. Gouy WWW-Query: An on-line retrieval system for biological sequence banks Biochimie 78 1996 364 369
    • (1996) Biochimie , vol.78 , pp. 364-369
    • Perrière, G.1    Gouy, M.2
  • 28
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • The Arabidopsis Genome Initiative Analysis of the genome sequence of the flowering plant Arabidopsis thaliana Nature 408 2000 796 815
    • (2000) Nature , vol.408 , pp. 796-815
    • Arabidopsis Genome Initiative, T.1
  • 29
    • 1942485914 scopus 로고    scopus 로고
    • Functional divergence in tandemly duplicated Arabidopsis thaliana trypsin inhibitor genes
    • M.J. Clauss, and T. Mitchell-Olds Functional divergence in tandemly duplicated Arabidopsis thaliana trypsin inhibitor genes Genetics 166 2004 1419 1436
    • (2004) Genetics , vol.166 , pp. 1419-1436
    • Clauss, M.J.1    Mitchell-Olds, T.2
  • 31
    • 0031401130 scopus 로고    scopus 로고
    • A plant chloroplast glutamyl proteinase
    • W.A. Laing, and J.T. Christeller A plant chloroplast glutamyl proteinase Plant Physiol. 114 1997 715 722
    • (1997) Plant Physiol. , vol.114 , pp. 715-722
    • Laing, W.A.1    Christeller, J.T.2
  • 32
    • 0034859320 scopus 로고    scopus 로고
    • A high molecular weight glutamyl endopeptidase and its endogenous inhibitors from cucumber leaves
    • Y. Yamauchi, Y. Ejiri, T. Sugimoto, K. Sueyoshi, Y. Oji, and K. Tanaka A high molecular weight glutamyl endopeptidase and its endogenous inhibitors from cucumber leaves J. Biochem. 130 2001 257 261
    • (2001) J. Biochem. , vol.130 , pp. 257-261
    • Yamauchi, Y.1    Ejiri, Y.2    Sugimoto, T.3    Sueyoshi, K.4    Oji, Y.5    Tanaka, K.6
  • 33
    • 0024110460 scopus 로고
    • Ethylene regulated expression of a tomato fruit ripening gene encoding a proteinase inhibitor I with a glutamic residue at the reactive site
    • L.J. Margossian, A.D. Federman, J.J. Giovannoni, and R.L. Fischer Ethylene regulated expression of a tomato fruit ripening gene encoding a proteinase inhibitor I with a glutamic residue at the reactive site Proc. Natl. Acad. Sci. USA 85 1988 8012 8016
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8012-8016
    • Margossian, L.J.1    Federman, A.D.2    Giovannoni, J.J.3    Fischer, R.L.4
  • 34
    • 0025478627 scopus 로고
    • Isolation and characterizationof a proteinaceous inhibitor of microbial proteinases induced during the hypersensitive reaction of tobacco to tobacco mosaic virus
    • P. Geoffroy, M. Legrand, and B. Fritig Isolation and characterizationof a proteinaceous inhibitor of microbial proteinases induced during the hypersensitive reaction of tobacco to tobacco mosaic virus Mol. Plant-Microbe Interact. 3 1990 327 333
    • (1990) Mol. Plant-Microbe Interact. , vol.3 , pp. 327-333
    • Geoffroy, P.1    Legrand, M.2    Fritig, B.3
  • 35
    • 0025948380 scopus 로고
    • Purification and amino acid sequence of a bitter gourd inhibitor against an acidic amino acid-specific endopeptidase of Streptomyces griseus
    • F. Ogata, T. Miyata, N. Fujii, N. Yoshida, K. Noda, S. Makisumi, and A. Ito Purification and amino acid sequence of a bitter gourd inhibitor against an acidic amino acid-specific endopeptidase of Streptomyces griseus J. Biol. Chem. 266 1991 16715 16721
    • (1991) J. Biol. Chem. , vol.266 , pp. 16715-16721
    • Ogata, F.1    Miyata, T.2    Fujii, N.3    Yoshida, N.4    Noda, K.5    Makisumi, S.6    Ito, A.7
  • 36
    • 0027351678 scopus 로고
    • Isolation and characterization of a cDNA that encodes a novel proteinase inhibitor I from a tobacco genetic tumor
    • T. Fujita, H. Kouchi, T. Ichikawa, and K. Syono Isolation and characterization of a cDNA that encodes a novel proteinase inhibitor I from a tobacco genetic tumor Plant Cell Physiol. 34 1993 137 142
    • (1993) Plant Cell Physiol. , vol.34 , pp. 137-142
    • Fujita, T.1    Kouchi, H.2    Ichikawa, T.3    Syono, K.4
  • 37
    • 0027570517 scopus 로고
    • Tobacco proteinase inhibitor I genes are locally, but not systemically induced by stress
    • H.J. Linthorst, F.T. Brederode, C. van der Does, and J.F. Bol Tobacco proteinase inhibitor I genes are locally, but not systemically induced by stress Plant Mol. Biol. 21 1993 985 992
    • (1993) Plant Mol. Biol. , vol.21 , pp. 985-992
    • Linthorst, H.J.1    Brederode, F.T.2    Van Der Does, C.3    Bol, J.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.