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Volumn 52, Issue 5, 2004, Pages 1350-1356

Cloning, Functional Expression, and Characterization of Cystatin in Sesame Seed

Author keywords

Cystatin; Cysteine protease inhibitor; Phytocystatin; Seed; Sesame

Indexed keywords

CELL EXTRACT; CYSTATIN; CYSTEINE PROTEINASE INHIBITOR; DNA FRAGMENT; PAPAIN;

EID: 1542286927     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf034989v     Document Type: Article
Times cited : (38)

References (36)
  • 1
    • 0037164073 scopus 로고    scopus 로고
    • Plant seed cystatins and their target enzymes of endogenous and exogenous origin
    • Arai, S.; Matsumoto, I.; Emori, Y.; Abe, K. Plant seed cystatins and their target enzymes of endogenous and exogenous origin. J. Agric. Food Chem. 2002, 50, 6612-6617.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 6612-6617
    • Arai, S.1    Matsumoto, I.2    Emori, Y.3    Abe, K.4
  • 2
    • 0030918546 scopus 로고    scopus 로고
    • Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
    • Turk, B.; Turk, V.; Turk, D. Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol. Chem. 1997, 378, 141-150.
    • (1997) Biol. Chem. , vol.378 , pp. 141-150
    • Turk, B.1    Turk, V.2    Turk, D.3
  • 3
    • 0032211213 scopus 로고    scopus 로고
    • Structural and phylogenetic relationships among plant and animal cystatins
    • Margis, R.; Reis, E. M.; Villeret, V. Structural and phylogenetic relationships among plant and animal cystatins. Arch. Biochem. Biophys. 1998, 359, 24-30.
    • (1998) Arch. Biochem. Biophys. , vol.359 , pp. 24-30
    • Margis, R.1    Reis, E.M.2    Villeret, V.3
  • 4
    • 0031013054 scopus 로고    scopus 로고
    • Friends and relations of the cystatin superfamily-new members and their evolution
    • Brown, W. M.; Dziegielewska, K. M. Friends and relations of the cystatin superfamily-new members and their evolution. Protein Sci. 1997, 6, 5-12.
    • (1997) Protein Sci. , vol.6 , pp. 5-12
    • Brown, W.M.1    Dziegielewska, K.M.2
  • 5
    • 0034610303 scopus 로고    scopus 로고
    • Three-dimensional structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica
    • Nagata, K.; Kudo, N.; Abe, K.; Arai, S.; Tanokura, M. Three-dimensional structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica. Biochemistry 2000, 39, 14753-14760.
    • (2000) Biochemistry , vol.39 , pp. 14753-14760
    • Nagata, K.1    Kudo, N.2    Abe, K.3    Arai, S.4    Tanokura, M.5
  • 6
    • 0023657047 scopus 로고
    • Molecular cloning of a cysteine proteinase inhitor of rice (oryzacystatin)-Homology with animal cystatins and transient expression in the ripening process of rice seed
    • Abe, K.; Emori, Y.; Kondo, H.; Suzuki, K.; Arai, S. Molecular cloning of a cysteine proteinase inhitor of rice (oryzacystatin)-Homology with animal cystatins and transient expression in the ripening process of rice seed. J. Biol. Chem. 1987, 262, 16793-16797.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16793-16797
    • Abe, K.1    Emori, Y.2    Kondo, H.3    Suzuki, K.4    Arai, S.5
  • 7
    • 0028814328 scopus 로고
    • Regulation of protein degradation
    • Callis, J. Regulation of protein degradation. Plant Cell 1995, 7, 845-857.
    • (1995) Plant Cell , vol.7 , pp. 845-857
    • Callis, J.1
  • 8
    • 0033101490 scopus 로고    scopus 로고
    • The involvement of cysteine proteases and protease inhibitor genes in programmed cell death in plants
    • Solomon, M.; Belengh, B.; Delledonne, M.; Levine, A. The involvement of cysteine proteases and protease inhibitor genes in programmed cell death in plants. Plant Cell 1999, 11, 431-444.
    • (1999) Plant Cell , vol.11 , pp. 431-444
    • Solomon, M.1    Belengh, B.2    Delledonne, M.3    Levine, A.4
  • 9
    • 0033083491 scopus 로고    scopus 로고
    • Expression of cysteine proteinase during developmental events associated with programmed cell death in brinjal
    • Xu, F.-X.; Chye, M.-L. Expression of cysteine proteinase during developmental events associated with programmed cell death in brinjal. Plant J. 1999, 17, 321-327.
    • (1999) Plant J. , vol.17 , pp. 321-327
    • Xu, F.-X.1    Chye, M.-L.2
  • 11
    • 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.; Gomez-Lim, M. A. The use of cysteine proteinase inhibitors to engineer resistance against potyviruses in transgenic tobacco plants. Nat. Biotechnol. 1999, 17, 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
  • 12
    • 0035211604 scopus 로고    scopus 로고
    • Expression pattern and deposition of three storage proteins, 11S globulin, 2S albumin and 7S globulin in maturing sesame seeds
    • Tai, S. S. K.; Lee, T. T. T.; Tsai, C. C. Y.; Yiu, T.-J.; Tzen, J. T. C. Expression pattern and deposition of three storage proteins, 11S globulin, 2S albumin and 7S globulin in maturing sesame seeds. Plant Physiol. Biochem. 2001, 39, 981-992.
    • (2001) Plant Physiol. Biochem. , vol.39 , pp. 981-992
    • Tai, S.S.K.1    Lee, T.T.T.2    Tsai, C.C.Y.3    Yiu, T.-J.4    Tzen, J.T.C.5
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0031936579 scopus 로고    scopus 로고
    • Coexistence of both oleosin isoforms on the surface of seed oil bodies and their individual stabilization to the organelle
    • Tzen, J. T. C.; Chuang, R. L. C.; Chen, J. C. F.; Wu, L. S. H. Coexistence of both oleosin isoforms on the surface of seed oil bodies and their individual stabilization to the organelle. J. Biochem. (Tokyo) 1998, 123, 319-324.
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 319-324
    • Tzen, J.T.C.1    Chuang, R.L.C.2    Chen, J.C.F.3    Wu, L.S.H.4
  • 16
    • 0032169151 scopus 로고    scopus 로고
    • Identification of three unique proteins in seed oil bodies of sesame
    • Chen, E. C. F.; Tai, S. S. K.; Peng, C.-C.; Tzen, J. T. C. Identification of three unique proteins in seed oil bodies of sesame. Plant Cell Physiol. 1998, 39, 935-941.
    • (1998) Plant Cell Physiol. , vol.39 , pp. 935-941
    • Chen, E.C.F.1    Tai, S.S.K.2    Peng, C.-C.3    Tzen, J.T.C.4
  • 18
    • 0035533230 scopus 로고    scopus 로고
    • Properties of cysteine proteinase inhibitors from black gram and rice bean
    • Benjakul, S.; Visessanguan, W.; An, H. Properties of cysteine proteinase inhibitors from black gram and rice bean. J. Food Biochem. 2001, 25, 211-227.
    • (2001) J. Food Biochem. , vol.25 , pp. 211-227
    • Benjakul, S.1    Visessanguan, W.2    An, H.3
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 0015338074 scopus 로고
    • A new assay for cathepsin B1 and other thio proteinases
    • Barrett, A. J. A new assay for cathepsin B1 and other thio proteinases. Anal. Biochem. 1972, 47, 280-293.
    • (1972) Anal. Biochem. , vol.47 , pp. 280-293
    • Barrett, A.J.1
  • 21
    • 0028093536 scopus 로고
    • Corn cystatin I expressed in Escherichia coli: Investigation of its inhibitory profile and occurrence in corn kernels
    • Abe, M.; Abe, K.; Iwabuchi, K.; Domoto, C.; Arai, S. Corn cystatin I expressed in Escherichia coli: investigation of its inhibitory profile and occurrence in corn kernels. J. Biochem. (Tokyo) 1994, 116, 488-492.
    • (1994) J. Biochem. (Tokyo) , vol.116 , pp. 488-492
    • Abe, M.1    Abe, K.2    Iwabuchi, K.3    Domoto, C.4    Arai, S.5
  • 22
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • Dixon, M. The determination of enzyme inhibitor constants. Biochem. J. 1953, 55, 170-171.
    • (1953) Biochem. J. , vol.55 , pp. 170-171
    • Dixon, M.1
  • 23
    • 0034857353 scopus 로고    scopus 로고
    • An electroblotting, two-step procedure for the detection of proteinases and the study of proteinase/inhibitor complexes in gelatin-containing polyacrylamide gels
    • Visal-Shah, S.; Vrain, T. C.; Yelle, S.; Nguyen-Quoc, B.; Michaud, D. An electroblotting, two-step procedure for the detection of proteinases and the study of proteinase/inhibitor complexes in gelatin-containing polyacrylamide gels. Electrophoresis 2001, 22, 2646-2652.
    • (2001) Electrophoresis , vol.22 , pp. 2646-2652
    • Visal-Shah, S.1    Vrain, T.C.2    Yelle, S.3    Nguyen-Quoc, B.4    Michaud, D.5
  • 24
    • 0024278653 scopus 로고
    • 2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of the cystatin superfamily
    • 2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of the cystatin superfamily. J. Biol. Chem. 1988, 262, 7655-7659.
    • (1988) J. Biol. Chem. , vol.262 , pp. 7655-7659
    • Abe, K.1    Emori, Y.2    Kondo, H.3    Arai, S.4    Suzuki, K.5
  • 25
    • 0029762217 scopus 로고    scopus 로고
    • Soyacystatin, a novel cysteine proteinase inhibitor in soybean, is distinct in protein structure and gene organization from other cystatins of animal and plant origin
    • Misaka, T.; Kuroda, M.; Iwabuchi, K.; Abe, K.; Arai, S. Soyacystatin, a novel cysteine proteinase inhibitor in soybean, is distinct in protein structure and gene organization from other cystatins of animal and plant origin. Eur. J. Biochem. 1996, 240, 609-614.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 609-614
    • Misaka, T.1    Kuroda, M.2    Iwabuchi, K.3    Abe, K.4    Arai, S.5
  • 26
    • 0030267548 scopus 로고    scopus 로고
    • Proteolysis in plants: Mechanisms and functions
    • Vierstra, R. D. Proteolysis in plants: Mechanisms and functions. Plant Mol. Biol. 1996, 32, 275-302.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 275-302
    • Vierstra, R.D.1
  • 27
    • 0001064980 scopus 로고    scopus 로고
    • Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds
    • Müntz, K. Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds. J. Exp. Bot. 1996, 47, 605-622.
    • (1996) J. Exp. Bot. , vol.47 , pp. 605-622
    • Müntz, K.1
  • 28
    • 0034846865 scopus 로고    scopus 로고
    • Stored proteinases and the initiation of storage protein mobilization in seeds during germination and seedling growth
    • Müntz, K.; Belozersky, M. A.; Dunaevsky, Y. E.; Schlereth, A.; Tiedemann, J. Stored proteinases and the initiation of storage protein mobilization in seeds during germination and seedling growth. J. Exp. Bot. 2001, 52, 1741-1752.
    • (2001) J. Exp. Bot. , vol.52 , pp. 1741-1752
    • Müntz, K.1    Belozersky, M.A.2    Dunaevsky, Y.E.3    Schlereth, A.4    Tiedemann, J.5
  • 29
    • 0035040254 scopus 로고    scopus 로고
    • Stored cysteine proteinases start globulin mobilization in protein bodies of embryonic axes and cotyledons during vetch (Vicia sativa L.) seed germination
    • Schelereth, A.; Standhardt, D.; Mock, H.-P.; Müntz, K. Stored cysteine proteinases start globulin mobilization in protein bodies of embryonic axes and cotyledons during vetch (Vicia sativa L.) seed germination. Planta 2001, 212, 718-727.
    • (2001) Planta , vol.212 , pp. 718-727
    • Schelereth, A.1    Standhardt, D.2    Mock, H.-P.3    Müntz, K.4
  • 31
    • 0030296222 scopus 로고    scopus 로고
    • Differential expression of soybean cysteine proteinase inhibitor genes during development and in response to wounding and methyl jasmonate
    • Botella, M. A.; Xu, Y.; Prabha, T. N.; Zhao, Y.; Naraimhan, M. L.; Wilson, K. A.; Nielsen, S. S.; Bressan, R. A.; Hasegawa, P. M. Differential expression of soybean cysteine proteinase inhibitor genes during development and in response to wounding and methyl jasmonate. Plant Physiol. 1996, 112, 1201-1210.
    • (1996) Plant Physiol. , vol.112 , pp. 1201-1210
    • Botella, M.A.1    Xu, Y.2    Prabha, T.N.3    Zhao, Y.4    Naraimhan, M.L.5    Wilson, K.A.6    Nielsen, S.S.7    Bressan, R.A.8    Hasegawa, P.M.9
  • 32
    • 0342288677 scopus 로고    scopus 로고
    • Biotic and abiotic stress can induce cystatin expression in chestnut
    • Pernas, M.; Sanchez-Mong, R.; Salcedo, G. Biotic and abiotic stress can induce cystatin expression in chestnut. FEBS Lett. 2000, 467, 206-210.
    • (2000) FEBS Lett. , vol.467 , pp. 206-210
    • Pernas, M.1    Sanchez-Mong, R.2    Salcedo, G.3
  • 33
    • 1542279127 scopus 로고    scopus 로고
    • Oryzacystatin I expression in transformed tobacco produces a conditional growth phenotype and enhances chilling tolerance
    • Van der Vyver, C.; Schneidereit, J.; Driscoll, S.; Turner, J.; Kunert, K.; Foyer, C. H. Oryzacystatin I expression in transformed tobacco produces a conditional growth phenotype and enhances chilling tolerance. Plant Biotechnol. J. 2003, 1, 101-112.
    • (2003) Plant Biotechnol. J. , vol.1 , pp. 101-112
    • Van Der Vyver, C.1    Schneidereit, J.2    Driscoll, S.3    Turner, J.4    Kunert, K.5    Foyer, C.H.6
  • 34
    • 0037134640 scopus 로고    scopus 로고
    • Enhanced expression of chicken cystatin as a thioredoxin fusion form in Escherichia coli AD494(DE3)pLysS and its effect on the prevention of surimi gel softening
    • Jiang, S.-T.; Tzeng, S.-S.; Wu, W.-T.; Chen, G.-H. Enhanced expression of chicken cystatin as a thioredoxin fusion form in Escherichia coli AD494(DE3)pLysS and its effect on the prevention of surimi gel softening. J. Agric. Food Chem. 2002, 50, 3731-3737.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 3731-3737
    • Jiang, S.-T.1    Tzeng, S.-S.2    Wu, W.-T.3    Chen, G.-H.4
  • 35
    • 0033213638 scopus 로고    scopus 로고
    • Cloning and secondary structure analysis of caleosin, a unique calcium-binding protein in oil bodies of plant seeds
    • Chen, J. C. F.; Tsai, C. C. Y.; Tzen, J. T. C. Cloning and secondary structure analysis of caleosin, a unique calcium-binding protein in oil bodies of plant seeds. Plant Cell Physiol. 1999, 40, 1079-1086.
    • (1999) Plant Cell Physiol. , vol.40 , pp. 1079-1086
    • Chen, J.C.F.1    Tsai, C.C.Y.2    Tzen, J.T.C.3
  • 36
    • 0036010643 scopus 로고    scopus 로고
    • Stereoleosin, a sterol-binding dehydrogenase in seed oil bodies
    • Lin, L.-J.; Tai, S. S. K.; Peng, C.-C.; Tzen, J. T. C. Stereoleosin, a sterol-binding dehydrogenase in seed oil bodies. Plant Physiol. 2002, 128, 1200-1211.
    • (2002) Plant Physiol. , vol.128 , pp. 1200-1211
    • Lin, L.-J.1    Tai, S.S.K.2    Peng, C.-C.3    Tzen, J.T.C.4


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