메뉴 건너뛰기




Volumn 57, Issue , 2012, Pages 181-192

Recombinant expression and biochemical characterization of sugarcane legumain

Author keywords

Cystatin; Expression analysis; Legumain; Phytohormone response; Sugarcane; Sugarcane development; Vacuolar processing enzyme

Indexed keywords

ABSCISIC ACID; CYSTEINE PROTEINASE; LEGUMAIN; PHYTOHORMONE; VACUOLAR PROCESSING ENZYME;

EID: 84862289740     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2012.05.020     Document Type: Article
Times cited : (15)

References (68)
  • 1
    • 0025986480 scopus 로고
    • A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into mature forms
    • Hara-Nishimura I., Inoue K., Nishimura M. A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into mature forms. FEBS Lett. 1991, 294:89-94.
    • (1991) FEBS Lett. , vol.294 , pp. 89-94
    • Hara-Nishimura, I.1    Inoue, K.2    Nishimura, M.3
  • 2
    • 0032970657 scopus 로고    scopus 로고
    • Vacuolar processing enzyme is self-catalytically activated by sequential removal of the C-terminal and N-terminal propeptides
    • Hiraiwa N., Nishimura M., Hara-Nishimura I. Vacuolar processing enzyme is self-catalytically activated by sequential removal of the C-terminal and N-terminal propeptides. FEBS Lett. 1999, 447:213-216.
    • (1999) FEBS Lett. , vol.447 , pp. 213-216
    • Hiraiwa, N.1    Nishimura, M.2    Hara-Nishimura, I.3
  • 3
    • 0036676947 scopus 로고    scopus 로고
    • Legumains and their functions in plants
    • Müntz K., Shutov A.D. Legumains and their functions in plants. Trends Plant Sci. 2002, 7:340-344.
    • (2002) Trends Plant Sci. , vol.7 , pp. 340-344
    • Müntz, K.1    Shutov, A.D.2
  • 4
    • 0036005912 scopus 로고    scopus 로고
    • Activation of Arabidopsis vacuolar processing enzyme by self-catalytic removal of an auto-inhibitory domain of the C-terminal propeptide
    • Kuroyanagi M., Nishimura M., Hara-Nishimura I. Activation of Arabidopsis vacuolar processing enzyme by self-catalytic removal of an auto-inhibitory domain of the C-terminal propeptide. Plant Cell Physiol. 2002, 43:143-151.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 143-151
    • Kuroyanagi, M.1    Nishimura, M.2    Hara-Nishimura, I.3
  • 5
    • 0029328357 scopus 로고
    • Seed storage proteins: structures and biosynthesis
    • Shewry P.R., Napier J.A., Tatham A.S. Seed storage proteins: structures and biosynthesis. Plant Cell 1995, 7:945-956.
    • (1995) Plant Cell , vol.7 , pp. 945-956
    • Shewry, P.R.1    Napier, J.A.2    Tatham, A.S.3
  • 8
  • 9
    • 0033883450 scopus 로고    scopus 로고
    • Comparison of globulin mobilization and cysteine proteinases in embryonic axes and cotyledons during germination and seedling growth of vetch (Vicia sativa L.)
    • Schlereth A., Becker C., Horstmann C., Tiedemann J., Müntz K. Comparison of globulin mobilization and cysteine proteinases in embryonic axes and cotyledons during germination and seedling growth of vetch (Vicia sativa L.). J. Exp. Bot. 2000, 51:1423-1433.
    • (2000) J. Exp. Bot. , vol.51 , pp. 1423-1433
    • Schlereth, A.1    Becker, C.2    Horstmann, C.3    Tiedemann, J.4    Müntz, K.5
  • 10
    • 5144228267 scopus 로고    scopus 로고
    • A comparative study of the role of the major proteinases of germinated common bean (Phaseolus vulgaris L.) and soybean (Glycine max (L.) Merrill) seeds in the degradation of their storage proteins
    • Zakharov A., Carchilan M., Stepurina T., Rotari V., Wilson K., Vaintraub I. A comparative study of the role of the major proteinases of germinated common bean (Phaseolus vulgaris L.) and soybean (Glycine max (L.) Merrill) seeds in the degradation of their storage proteins. J. Exp. Bot. 2004, 55:2241-2249.
    • (2004) J. Exp. Bot. , vol.55 , pp. 2241-2249
    • Zakharov, A.1    Carchilan, M.2    Stepurina, T.3    Rotari, V.4    Wilson, K.5    Vaintraub, I.6
  • 11
    • 0032991832 scopus 로고    scopus 로고
    • Molecular cloning and characterization of Vigna mungo processing enzyme 1 (VmPE-1), an asparaginyl endopeptidase
    • Okamoto T., Minamikawa T. Molecular cloning and characterization of Vigna mungo processing enzyme 1 (VmPE-1), an asparaginyl endopeptidase. Plant Mol. Biol. 1999, 39:63-73.
    • (1999) Plant Mol. Biol. , vol.39 , pp. 63-73
    • Okamoto, T.1    Minamikawa, T.2
  • 14
    • 33846205136 scopus 로고    scopus 로고
    • Modification of nitrogen remobilization, grain fill and leaf senescence in maize (Zea mays) by transposon insertional mutagenesis in a protease gene
    • Donnison I.S., Gay A.P., Thomas H., Edwards K.J., Edwards D., James C.L., Thomas A.M., Ougham H.J. Modification of nitrogen remobilization, grain fill and leaf senescence in maize (Zea mays) by transposon insertional mutagenesis in a protease gene. New Phytol. 2007, 173:481-494.
    • (2007) New Phytol. , vol.173 , pp. 481-494
    • Donnison, I.S.1    Gay, A.P.2    Thomas, H.3    Edwards, K.J.4    Edwards, D.5    James, C.L.6    Thomas, A.M.7    Ougham, H.J.8
  • 15
    • 0033166888 scopus 로고    scopus 로고
    • Vacuolar processing enzyme is up-regulated in the lytic vacuoles of vegetative tissues during senescence and under various stressed conditions
    • Kinoshita T., Yamada K., Hiraiwa N., Kondo M., Nishimura M., Hara-Nishimura I. Vacuolar processing enzyme is up-regulated in the lytic vacuoles of vegetative tissues during senescence and under various stressed conditions. Plant J. 1999, 19:43-53.
    • (1999) Plant J. , vol.19 , pp. 43-53
    • Kinoshita, T.1    Yamada, K.2    Hiraiwa, N.3    Kondo, M.4    Nishimura, M.5    Hara-Nishimura, I.6
  • 17
    • 0036233856 scopus 로고    scopus 로고
    • The peptidase zymogen proregions: nature's way of preventing undesired activation and proteolysis
    • Lazure C. The peptidase zymogen proregions: nature's way of preventing undesired activation and proteolysis. Curr. Pharm. Des. 2002, 8:511-531.
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 511-531
    • Lazure, C.1
  • 19
    • 67349130075 scopus 로고    scopus 로고
    • Developmentally linked changes in proteases and protease inhibitors suggest a role for potato multicystatin in regulating protein content of potato tubers
    • Weeda S.M., Mohan Kumar G.N., Richard Knowles N. Developmentally linked changes in proteases and protease inhibitors suggest a role for potato multicystatin in regulating protein content of potato tubers. Planta 2009, 230:73-84.
    • (2009) Planta , vol.230 , pp. 73-84
    • Weeda, S.M.1    Mohan Kumar, G.N.2    Richard Knowles, N.3
  • 21
    • 0025817602 scopus 로고
    • The cystatins: protein inhibitors of cysteine proteinases
    • Turk V., Bode W. The cystatins: protein inhibitors of cysteine proteinases. FEBS Lett. 1991, 285:213-219.
    • (1991) FEBS Lett. , vol.285 , pp. 213-219
    • Turk, V.1    Bode, W.2
  • 22
    • 33744915019 scopus 로고    scopus 로고
    • Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site: a novel clue for the role of cystatin M/E in epidermal cornification
    • Cheng T., Hitomi K., Van Vlijmen-Willems I.M., De Jongh G.J., Yamamoto K., Nishi K., Watts C., Reinheckel T., Schalkwijk J., Zeeuwen P.L. Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site: a novel clue for the role of cystatin M/E in epidermal cornification. J. Biol. Chem. 2006, 281:15893-15899.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15893-15899
    • Cheng, T.1    Hitomi, K.2    Van Vlijmen-Willems, I.M.3    De Jongh, G.J.4    Yamamoto, K.5    Nishi, K.6    Watts, C.7    Reinheckel, T.8    Schalkwijk, J.9    Zeeuwen, P.L.10
  • 23
    • 34250357224 scopus 로고    scopus 로고
    • Carboxy terminal extended phytocystatins are bifunctional inhibitors of papain and legumain cysteine proteinases
    • Martinez M., Diaz-Mendoza M., Carrillo L., Diaz I. Carboxy terminal extended phytocystatins are bifunctional inhibitors of papain and legumain cysteine proteinases. FEBS Lett. 2007, 581:2914-2918.
    • (2007) FEBS Lett. , vol.581 , pp. 2914-2918
    • Martinez, M.1    Diaz-Mendoza, M.2    Carrillo, L.3    Diaz, I.4
  • 25
    • 4444251748 scopus 로고    scopus 로고
    • Identification of differentially expressed transcripts from maturing stem of sugarcane by in silico analysis of stem expressed sequence tags and gene expression profiling
    • Casu R.E., Dimmock C.M., Chapman S.C., Grof C.P., Mcintyre C.L., Bonnett G.D., Manners J.M. Identification of differentially expressed transcripts from maturing stem of sugarcane by in silico analysis of stem expressed sequence tags and gene expression profiling. Plant Mol. Biol. 2004, 54:503-517.
    • (2004) Plant Mol. Biol. , vol.54 , pp. 503-517
    • Casu, R.E.1    Dimmock, C.M.2    Chapman, S.C.3    Grof, C.P.4    Mcintyre, C.L.5    Bonnett, G.D.6    Manners, J.M.7
  • 29
    • 0032435254 scopus 로고    scopus 로고
    • Identification of the active site of legumain links it to caspases clostripain and gingipains in a new clan of cysteine endopeptidases
    • Chen J.M., Rawlings N.D., Stevens R.A.E., Barret A.J. Identification of the active site of legumain links it to caspases clostripain and gingipains in a new clan of cysteine endopeptidases. FEBS Lett. 1998, 441:361-365.
    • (1998) FEBS Lett. , vol.441 , pp. 361-365
    • Chen, J.M.1    Rawlings, N.D.2    Stevens, R.A.E.3    Barret, A.J.4
  • 30
    • 0034925333 scopus 로고    scopus 로고
    • Legumain forms form plants and animals differ in their specificity
    • Rotari V.I., Dando P.M., Barrett A.J. Legumain forms form plants and animals differ in their specificity. Biol. Chem. 2001, 382:953-959.
    • (2001) Biol. Chem. , vol.382 , pp. 953-959
    • Rotari, V.I.1    Dando, P.M.2    Barrett, A.J.3
  • 32
    • 34347371788 scopus 로고    scopus 로고
    • A bioinformatic approach to the identification of a conserved domain in a sugarcane legumain that directs GFP to the lytic vacuole
    • Jackson M.A., Rae A.L., Casu R.E., Grof C.P.L., Bonnett G.D., Maclean D.J. A bioinformatic approach to the identification of a conserved domain in a sugarcane legumain that directs GFP to the lytic vacuole. Funct. Plant Biol. 2007, 34:633-644.
    • (2007) Funct. Plant Biol. , vol.34 , pp. 633-644
    • Jackson, M.A.1    Rae, A.L.2    Casu, R.E.3    Grof, C.P.L.4    Bonnett, G.D.5    Maclean, D.J.6
  • 33
  • 34
    • 0141755165 scopus 로고    scopus 로고
    • Multistep autoactivation of asparaginyl andopeptidase in vitro and in vivo
    • Li D.N., Matthews S.P., Antoniou A.N., Mazzeo D., Watts C. Multistep autoactivation of asparaginyl andopeptidase in vitro and in vivo. J. Biol. Chem. 2003, 278:38980-38990.
    • (2003) J. Biol. Chem. , vol.278 , pp. 38980-38990
    • Li, D.N.1    Matthews, S.P.2    Antoniou, A.N.3    Mazzeo, D.4    Watts, C.5
  • 35
    • 0027477474 scopus 로고
    • Asparaginyl endopeptidase of jack bean seeds: purification characterization and high utility in protein sequence analysis
    • Abe Y., Shirane K., Yokosawa H., Matsushita H., Mitta M., Kato I., Ishii S. Asparaginyl endopeptidase of jack bean seeds: purification characterization and high utility in protein sequence analysis. J. Biol. Chem. 1993, 268:3525-3529.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3525-3529
    • Abe, Y.1    Shirane, K.2    Yokosawa, H.3    Matsushita, H.4    Mitta, M.5    Kato, I.6    Ishii, S.7
  • 36
    • 0032582565 scopus 로고    scopus 로고
    • Autocatalytic activation of human legumain at aspartic acid residues
    • Halfon S., Patel S., Vega F., Zurawski S., Zurawski G. Autocatalytic activation of human legumain at aspartic acid residues. FEBS Lett. 1998, 438:114-118.
    • (1998) FEBS Lett. , vol.438 , pp. 114-118
    • Halfon, S.1    Patel, S.2    Vega, F.3    Zurawski, S.4    Zurawski, G.5
  • 37
    • 77957958245 scopus 로고    scopus 로고
    • Characterization of a legumain/vacuolar processing enzyme and YVADase activity in Papaver pollen
    • Bosch M., Poulter N.S., Perry R.M., Wilkins K.A., Franklin-Tong V.E. Characterization of a legumain/vacuolar processing enzyme and YVADase activity in Papaver pollen. Plant Mol. Biol. 2010, 74:381-393.
    • (2010) Plant Mol. Biol. , vol.74 , pp. 381-393
    • Bosch, M.1    Poulter, N.S.2    Perry, R.M.3    Wilkins, K.A.4    Franklin-Tong, V.E.5
  • 38
    • 0033101490 scopus 로고    scopus 로고
    • The involvement of cysteine proteases and protease inhibitor genes in the regulation of programmed cell death in plants
    • Solomon M., Belenghi B., Delledonne M., Menachem E., Levine A. The involvement of cysteine proteases and protease inhibitor genes in the regulation of programmed cell death in plants. Plant Cell 1999, 11:431-444.
    • (1999) Plant Cell , vol.11 , pp. 431-444
    • Solomon, M.1    Belenghi, B.2    Delledonne, M.3    Menachem, E.4    Levine, A.5
  • 39
    • 33644852137 scopus 로고    scopus 로고
    • Downregulation of Solanum americanum genes encoding proteinase inhibitor II causes defective seed development
    • Sin S.F., Yeung E.C., Chye M.L. Downregulation of Solanum americanum genes encoding proteinase inhibitor II causes defective seed development. Plant J. 2006, 45:58-70.
    • (2006) Plant J. , vol.45 , pp. 58-70
    • Sin, S.F.1    Yeung, E.C.2    Chye, M.L.3
  • 42
  • 43
    • 0038808989 scopus 로고    scopus 로고
    • A unique mechanism for protein processing and degradation in Arabidopsis thaliana
    • Rojo E., Zouhar J., Carter C., Kovaleva V., Raikhel N.V. A unique mechanism for protein processing and degradation in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 2003, 100:7389-7394.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7389-7394
    • Rojo, E.1    Zouhar, J.2    Carter, C.3    Kovaleva, V.4    Raikhel, N.V.5
  • 44
    • 79955091756 scopus 로고    scopus 로고
    • A soluble acid invertase is directed to the vacuole by a signal anchor mechanism
    • Rae A.L., Casu R.E., Perroux J.M., Jackson M.A., Grof C.P. A soluble acid invertase is directed to the vacuole by a signal anchor mechanism. J. Plant Physiol. 2011, 168:983-989.
    • (2011) J. Plant Physiol. , vol.168 , pp. 983-989
    • Rae, A.L.1    Casu, R.E.2    Perroux, J.M.3    Jackson, M.A.4    Grof, C.P.5
  • 45
    • 77950343440 scopus 로고    scopus 로고
    • Regulation of seed germination and seedling growth by an Arabidopsis phytocystatin isoform AtCYS6
    • Hwang J.E., Hong J.K., Je J.H., Lee K.O., Kim D.Y., Lee S.Y., Lim C.O. Regulation of seed germination and seedling growth by an Arabidopsis phytocystatin isoform AtCYS6. Plant Cell. Rep. 2009, 28:1623-1632.
    • (2009) Plant Cell. Rep. , vol.28 , pp. 1623-1632
    • Hwang, J.E.1    Hong, J.K.2    Je, J.H.3    Lee, K.O.4    Kim, D.Y.5    Lee, S.Y.6    Lim, C.O.7
  • 46
    • 0041851356 scopus 로고    scopus 로고
    • Identification cDNA cloning and possible roles of seed-specific rice asparaginyl endopeptidase REP-2
    • Kato H., Sutoh K., Minamikawa T. Identification cDNA cloning and possible roles of seed-specific rice asparaginyl endopeptidase REP-2. Planta 2003, 217:676-685.
    • (2003) Planta , vol.217 , pp. 676-685
    • Kato, H.1    Sutoh, K.2    Minamikawa, T.3
  • 47
    • 0037338198 scopus 로고    scopus 로고
    • A cathepsin B-like cysteine protease gene from Hordeum vulgare (gene CatB) induced by GA in aleurone cells is under circadian control in leaves
    • Martínez M., Rubio-Somoza I., Carbonero P., Díaz I. A cathepsin B-like cysteine protease gene from Hordeum vulgare (gene CatB) induced by GA in aleurone cells is under circadian control in leaves. J. Exp. Bot. 2003, 54:951-959.
    • (2003) J. Exp. Bot. , vol.54 , pp. 951-959
    • Martínez, M.1    Rubio-Somoza, I.2    Carbonero, P.3    Díaz, I.4
  • 49
    • 1442290968 scopus 로고    scopus 로고
    • The slow wound-response of gammaVPE is regulated by endogenous salicylic acid in Arabidopsis
    • Yamada K., Nishimura M., Hara-Nishimura I. The slow wound-response of gammaVPE is regulated by endogenous salicylic acid in Arabidopsis. Planta 2004, 218:599-605.
    • (2004) Planta , vol.218 , pp. 599-605
    • Yamada, K.1    Nishimura, M.2    Hara-Nishimura, I.3
  • 50
    • 0342288677 scopus 로고    scopus 로고
    • Biotic and abiotic stress can induce cystatin expression in chestnut
    • Pernas M., Sánchez-Monge 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    Sánchez-Monge, R.2    Salcedo, G.3
  • 53
    • 48149110148 scopus 로고    scopus 로고
    • Two cysteine proteinase inhibitors from Arabidopsis thaliana AtCYSa and AtCYSb increasing the salt drought oxidation and cold tolerance
    • Zhang X., Liu S., Takano T. Two cysteine proteinase inhibitors from Arabidopsis thaliana AtCYSa and AtCYSb increasing the salt drought oxidation and cold tolerance. Plant Mol. Biol. 2008, 68:131-143.
    • (2008) Plant Mol. Biol. , vol.68 , pp. 131-143
    • Zhang, X.1    Liu, S.2    Takano, T.3
  • 54
    • 77954533754 scopus 로고    scopus 로고
    • Distinct expression patterns of two Arabidopsis phytocystatin genes AtCYS1 and AtCYS2 during development and abiotic stresses
    • Hwang J.E., Hong J.K., Lim C.J., Chen H., Je J., Yang K.A., Kim D.Y., Choi Y.J., Lee S.Y., Lim C.O. Distinct expression patterns of two Arabidopsis phytocystatin genes AtCYS1 and AtCYS2 during development and abiotic stresses. Plant Cell Rep. 2010, 29:905-915.
    • (2010) Plant Cell Rep. , vol.29 , pp. 905-915
    • Hwang, J.E.1    Hong, J.K.2    Lim, C.J.3    Chen, H.4    Je, J.5    Yang, K.A.6    Kim, D.Y.7    Choi, Y.J.8    Lee, S.Y.9    Lim, C.O.10
  • 57
    • 0002886657 scopus 로고
    • Micropropagation of sugarcane (Saccharum spp.)
    • Lee T.S.G. Micropropagation of sugarcane (Saccharum spp.). Plant Cell Tissue Organ Cult. 1987, 10:47-55.
    • (1987) Plant Cell Tissue Organ Cult. , vol.10 , pp. 47-55
    • Lee, T.S.G.1
  • 61
    • 0034128691 scopus 로고    scopus 로고
    • DNA extraction method for screening yeast clones by PCR
    • Akada R., Murakane T., Nishizawa Y. DNA extraction method for screening yeast clones by PCR. Biotechniques 2000, 28:670-673.
    • (2000) Biotechniques , vol.28 , pp. 670-673
    • Akada, R.1    Murakane, T.2    Nishizawa, Y.3
  • 62
    • 0000544299 scopus 로고
    • A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels
    • Oakley B.R., Kirsch D.R., Morris N.R. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal. Biochem. 1980, 105:361-363.
    • (1980) Anal. Biochem. , vol.105 , pp. 361-363
    • Oakley, B.R.1    Kirsch, D.R.2    Morris, N.R.3
  • 63
    • 51649122509 scopus 로고    scopus 로고
    • Electroelution of proteins from polyacrylamide gels
    • Humana Press, Totowa, NJ, J.M. Walker (Ed.)
    • Jenö P., Horst M. Electroelution of proteins from polyacrylamide gels. The Protein Protocols Handbook 1996, 207-214. Humana Press, Totowa, NJ. J.M. Walker (Ed.).
    • (1996) The Protein Protocols Handbook , pp. 207-214
    • Jenö, P.1    Horst, M.2
  • 64
    • 85004377807 scopus 로고
    • Purification and some properties of dipeptidyl carboxypeptidase from Bacillus pumilus
    • Nagamori Y., Fujishima N., Okada S. Purification and some properties of dipeptidyl carboxypeptidase from Bacillus pumilus. Agric. Biol. Chem. 1990, 54:999-1005.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 999-1005
    • Nagamori, Y.1    Fujishima, N.2    Okada, S.3
  • 66
    • 0001396685 scopus 로고
    • The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions
    • Morrison J.F. The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions. TIBS 1982, 7:102-105.
    • (1982) TIBS , vol.7 , pp. 102-105
    • Morrison, J.F.1
  • 68
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • Pfaffl M.W., Horgan G.W., Dempfle L. Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic Acids Res. 2002, 30:e36.
    • (2002) Nucleic Acids Res. , vol.30
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.