메뉴 건너뛰기




Volumn 370, Issue 1, 2003, Pages 57-67

Ara12 subtilisin-like protease from Arabidopsis thaliana: Purification, substrate specificity and tissue localization

Author keywords

Apoplast; Pyrolysin; Serine endoprotease

Indexed keywords

BACTERIA; CELL CULTURE; HYDROPHOBICITY; IMMUNOLOGY; RNA; SUSPENSIONS (FLUIDS); TISSUE;

EID: 0037442529     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021125     Document Type: Article
Times cited : (57)

References (47)
  • 1
    • 0025998717 scopus 로고
    • Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteases
    • Siezen, R. J., de Vos, W. M., Leunissen, A. M. and Dijkstra, B. W. (1991) Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteases. Protein Eng. 4, 719-737
    • (1991) Protein Eng. , vol.4 , pp. 719-737
    • Siezen, R.J.1    De Vos, W.M.2    Leunissen, A.M.3    Dijkstra, B.W.4
  • 2
    • 0030896832 scopus 로고    scopus 로고
    • Subtilases: The superfamily of subtilisin-like serine proteases
    • Siezen, R. J. and Leunissen, J. A. M. (1997) Subtilases: the superfamily of subtilisin-like serine proteases. Protein Sci. 6, 501-523
    • (1997) Protein Sci. , vol.6 , pp. 501-523
    • Siezen, R.J.1    Leunissen, J.A.M.2
  • 3
    • 0030725756 scopus 로고    scopus 로고
    • Furin: A mammalian subtilisin/Kex2p-like endoprotease involved in processing a wide variety of precursor proteins
    • Nakayama, K. (1997) Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing a wide variety of precursor proteins. Biochem. J. 327, 625-635
    • (1997) Biochem. J. , vol.327 , pp. 625-635
    • Nakayama, K.1
  • 4
    • 0025733702 scopus 로고
    • Mammalian subtilisins: The long-sought dibasic processing endoproteases
    • Barr, P. J. (1991) Mammalian subtilisins: the long-sought dibasic processing endoproteases. Cell 66, 1-3
    • (1991) Cell , vol.66 , pp. 1-3
    • Barr, P.J.1
  • 5
    • 0343307146 scopus 로고    scopus 로고
    • Eukaryotic protein processing: Endoproteolysis of precursor proteins
    • Seidah, N. G. and Chretien, M. (1997) Eukaryotic protein processing: endoproteolysis of precursor proteins. Curr. Opin. Biotechnol. 8, 602-607
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 602-607
    • Seidah, N.G.1    Chretien, M.2
  • 6
    • 0032185770 scopus 로고    scopus 로고
    • Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells
    • Sakai, J., Rawson, R. B., Espenshade, P. J., Cheng, D., Seegmiller, A. C., Goldstein, J. L. and Brown, M. S. (1998) Molecular identification of the sterol-regulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells. Mol. Cell 2, 505-514
    • (1998) Mol. Cell , vol.2 , pp. 505-514
    • Sakai, J.1    Rawson, R.B.2    Espenshade, P.J.3    Cheng, D.4    Seegmiller, A.C.5    Goldstein, J.L.6    Brown, M.S.7
  • 8
    • 0033529545 scopus 로고    scopus 로고
    • Secreted Site-1 protease cleaves peptides corresponding to luminal loop of sterol regulatory element-binding proteins
    • Cheng, D., Espenshade, P. J., Slaughter, C. A., Jaen, J. C., Brown, M. S. and Goldstein, J. L. (1999) Secreted Site-1 protease cleaves peptides corresponding to luminal loop of sterol regulatory element-binding proteins. J. Biol. Chem. 274, 22805-22812
    • (1999) J. Biol. Chem. , vol.274 , pp. 22805-22812
    • Cheng, D.1    Espenshade, P.J.2    Slaughter, C.A.3    Jaen, J.C.4    Brown, M.S.5    Goldstein, J.L.6
  • 10
    • 0016678184 scopus 로고
    • Isolat on and characterization of a proteinase from the sarcocarp of melon fruit
    • Kaneda, M. and Tominaga, N. (1975) Isolat on and characterization of a proteinase from the sarcocarp of melon fruit. J. Biochem (Tokyo) 78, 1287-1296
    • (1975) J. Biochem. (Tokyo) , vol.78 , pp. 1287-1296
    • Kaneda, M.1    Tominaga, N.2
  • 11
    • 0028587825 scopus 로고
    • Cucumisin, a serine protease from melon fruits, shares structural homology with subtilisin and is generated from a large precursor
    • Yamagata, H., Masuzawa, T., Nagaoka, Y., (Ihnishi, T. and Iwasaki, T. (1994) Cucumisin, a serine protease from melon fruits, shares structural homology with subtilisin and is generated from a large precursor. J. Biol. Chem. 269, 32725-32731
    • (1994) J. Biol. Chem. , vol.269 , pp. 32725-32731
    • Yamagata, H.1    Masuzawa, T.2    Nagaoka, Y.3    Ihnishi, T.4    Iwasaki, T.5
  • 13
    • 0030970430 scopus 로고    scopus 로고
    • Identification of a new pathogen-induced member of the subtilisin-like processing protease family from plants
    • Tornero, P., Conejero, V. and Vera, P. (1997) Identification of a new pathogen-induced member of the subtilisin-like processing protease family from plants. J. Biol. Chem. 272, 14412-14419
    • (1997) J. Biol. Chem. , vol.272 , pp. 14412-14419
    • Tornero, P.1    Conejero, V.2    Vera, P.3
  • 14
    • 0031452632 scopus 로고    scopus 로고
    • Maturation and secretion of a serine proteinase is associated with events of late microsporogenesis
    • Taylor, A. A., Horsch, A., Rzepczyk, A., Hasenkampf, C. A. and Riggs, C. D. (1997) Maturation and secretion of a serine proteinase is associated with events of late microsporogenesis. Plant J. 12, 1261-1271
    • (1997) Plant J. , vol.12 , pp. 1261-1271
    • Taylor, A.A.1    Horsch, A.2    Rzepczyk, A.3    Hasenkampf, C.A.4    Riggs, C.D.5
  • 15
    • 0033104085 scopus 로고    scopus 로고
    • Characterisation of the subtilase gene family in tomato (Lycopersicon esculentum Mill.)
    • Meichtry, J., Amrhein, N. and Schaller, A. (1999) Characterisation of the subtilase gene family in tomato (Lycopersicon esculentum Mill.). Plant Mol. Biol. 39, 749-760
    • (1999) Plant Mol. Biol. , vol.39 , pp. 749-760
    • Meichtry, J.1    Amrhein, N.2    Schaller, A.3
  • 16
    • 0033067345 scopus 로고    scopus 로고
    • Isolation and characterization of cDNA clones corresponding with mRNAs that accumulate during auxin-induced lateral root formation
    • Neuteboom, L. W., Ng, J. M. Y., Kuyper, M. Clijdesdale, O. R., Hooykaas, P. J. J. and van der Zaal, B. J. (1999) Isolation and characterization of cDNA clones corresponding with mRNAs that accumulate during auxin-induced lateral root formation. Plant Mol. Biol. 39, 273-287
    • (1999) Plant Mol. Biol. , vol.39 , pp. 273-287
    • Neuteboom, L.W.1    Ng, J.M.Y.2    Kuyper, M.3    Clijdesdale, O.R.4    Hooykaas, P.J.J.5    Van Der Zaal, B.J.6
  • 17
    • 0033927031 scopus 로고    scopus 로고
    • Exploiting secondary growth in Arabidopsis. Construction of xylem and bark cDNA libraries and cloning of three xylem endopeptidases
    • Zhao, C. S., Johnson, B. J., Kositsup, B. and Beers, E. P. (2000) Exploiting secondary growth in Arabidopsis. Construction of xylem and bark cDNA libraries and cloning of three xylem endopeptidases. Plant Physiol. 23, 1185-1196
    • (2000) Plant Physiol. , vol.23 , pp. 1185-1196
    • Zhao, C.S.1    Johnson, B.J.2    Kositsup, B.3    Beers, E.P.4
  • 18
    • 0034193779 scopus 로고    scopus 로고
    • A subtilisin-like serine protease involved in the regulation of stomatal density and distribution in Arabidopsis thaliana
    • Berger, D. and Altmann, T. (2000) A subtilisin-like serine protease involved in the regulation of stomatal density and distribution in Arabidopsis thaliana. Genes Dev. 14, 1119-1131
    • (2000) Genes Dev. , vol.14 , pp. 1119-1131
    • Berger, D.1    Altmann, T.2
  • 19
    • 0035207824 scopus 로고    scopus 로고
    • A subtilisin-like serine protease is required for epidermal surface formation in Arabidopsis embryos and juvenile plants
    • Tanaka, H., Onouchi, H., Kondo, M., Hara-Nishimura, I., Nishimura, M., Machida, C. and Machida, Y. (2001) A subtilisin-like serine protease is required for epidermal surface formation in Arabidopsis embryos and juvenile plants. Development 128, 4681-4689
    • (2001) Development , vol.128 , pp. 4681-4689
    • Tanaka, H.1    Onouchi, H.2    Kondo, M.3    Hara-Nishimura, I.4    Nishimura, M.5    Machida, C.6    Machida, Y.7
  • 21
    • 0029310466 scopus 로고
    • A nodule-specific gene encoding a subtilisin-like protease is expressed in early stages of actinorhizal nodule development
    • Ribeiro, A., Akkermans, A. D. L., van Kammen, A., Bisseling, T. and Pawlowski, K. (1995) A nodule-specific gene encoding a subtilisin-like protease is expressed in early stages of actinorhizal nodule development. Plant Cell 7, 785-794
    • (1995) Plant Cell , vol.7 , pp. 785-794
    • Ribeiro, A.1    Akkermans, A.D.L.2    Van Kammen, A.3    Bisseling, T.4    Pawlowski, K.5
  • 22
    • 0033961794 scopus 로고    scopus 로고
    • Characterization of a Casuarina glauca nodule-specific subtilisin-like protease gene, a homolog of Alnus glutinosa ag12
    • Laplaze, L., Ribeiro, A., Franche, C., Duhoux, E., Auguy, F., Bogusz, D. and Pawlowski, K. (2000) Characterization of a Casuarina glauca nodule-specific subtilisin-like protease gene, a homolog of Alnus glutinosa ag12. Mol. Plant Microbe Interact 13, 113-117
    • (2000) Mol. Plant Microbe Interact. , vol.13 , pp. 113-117
    • Laplaze, L.1    Ribeiro, A.2    Franche, C.3    Duhoux, E.4    Auguy, F.5    Bogusz, D.6    Pawlowski, K.7
  • 23
    • 0033593221 scopus 로고    scopus 로고
    • A genomic cluster containing four differentially regulated subtilisin-like processing protease genes is in tomato plants
    • Jordá L., Coego, A., Conejero, V. and Vera, P. (1999) A genomic cluster containing four differentially regulated subtilisin-like processing protease genes is in tomato plants. J. Biol. Chem. 274, 2360-2365
    • (1999) J. Biol. Chem. , vol.274 , pp. 2360-2365
    • Jordá, L.1    Coego, A.2    Conejero, V.3    Vera, P.4
  • 24
    • 0027987123 scopus 로고
    • Identification of a 50 kDa systemin-binding protein in tomato plasma membranes having Kex2p-like properties
    • Schaller, A. and Ryan, C. A. (1994) Identification of a 50 kDa systemin-binding protein in tomato plasma membranes having Kex2p-like properties. Proc. Natl. Acad. Sci. U.S.A. 91, 11802-11806
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 11802-11806
    • Schaller, A.1    Ryan, C.A.2
  • 25
    • 0030210490 scopus 로고    scopus 로고
    • Characterisation of LRP, a leucine-rich repeal (LRR) protein from tomato plants that is processed during pathogenesis
    • Tornero, P., Mayda, E., Gomez, M. D., Canas, L., Conejero, V. and Vera, P. (1996) Characterisation of LRP, a leucine-rich repeal (LRR) protein from tomato plants that is processed during pathogenesis. Plant J. 10, 315-330
    • (1996) Plant J. , vol.10 , pp. 315-330
    • Tornero, P.1    Mayda, E.2    Gomez, M.D.3    Canas, L.4    Conejero, V.5    Vera, P.6
  • 26
    • 0030979341 scopus 로고    scopus 로고
    • Differential extraction and protein sequencing reveals major differences in patterns of primary cell wall proteins from plants
    • Robertson, D., Mitchell, G. P., Gilroy, J. S., Gerrish, C., Bolwell, G. P. and Slabas, A. R. (1997) Differential extraction and protein sequencing reveals major differences in patterns of primary cell wall proteins from plants. J. Biol. Chem. 272, 15841-15848
    • (1997) J. Biol. Chem. , vol.272 , pp. 15841-15848
    • Robertson, D.1    Mitchell, G.P.2    Gilroy, J.S.3    Gerrish, C.4    Bolwell, G.P.5    Slabas, A.R.6
  • 27
    • 0034278137 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a cDNA and a gene for subtilisin-like proteases from rice (Oryza sativa L.) and Arabidopsis thaliana
    • Yamagata, H., Uesugi, M., Saka, K., Iwasaki, T. and Aizono, Y. (2000) Molecular cloning and characterization of a cDNA and a gene for subtilisin-like proteases from rice (Oryza sativa L.) and Arabidopsis thaliana. Biosci. Biotechnol. Biochem. 64, 1947-1957
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 1947-1957
    • Yamagata, H.1    Uesugi, M.2    Saka, K.3    Iwasaki, T.4    Aizono, Y.5
  • 28
    • 0027143463 scopus 로고
    • Oxidative stimulation of glutathione synthesis in Arabidopsis thaliana suspension-cultures
    • May, M. J. and Leaver, C. J. (1993) Oxidative stimulation of glutathione synthesis in Arabidopsis thaliana suspension-cultures. Plant Physiol. 103, 621-627
    • (1993) Plant Physiol. , vol.103 , pp. 621-627
    • May, M.J.1    Leaver, C.J.2
  • 29
    • 0021738226 scopus 로고
    • Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes
    • Twining, S. S. (1984) Fluorescein isothiocyanate-labeled casein assay for proteolytic enzymes. Anal. Biochem. 143, 30-34
    • (1984) Anal. Biochem. , vol.143 , pp. 30-34
    • Twining, S.S.1
  • 30
    • 0025770925 scopus 로고
    • Anthrani amide and nitrotyrosine as a donor-acceptor pair in internally quenched fluorescent substrates for endopeptidases - Multicolumn peptide-synthesis of enzyme substrates for subtilisin Carlsberg and pepsin
    • Meldal, M. and Breddam, K. (1991) Anthrani amide and nitrotyrosine as a donor-acceptor pair in internally quenched fluorescent substrates for endopeptidases - multicolumn peptide-synthesis of enzyme substrates for subtilisin Carlsberg and pepsin. Anal. Biochem. 195, 141-147
    • (1991) Anal. Biochem. , vol.195 , pp. 141-147
    • Meldal, M.1    Breddam, K.2
  • 32
    • 0020345697 scopus 로고
    • Buffers of constant ionic strength for studying pH-dependent processes
    • Ellis, K. J. and Morrison, J. F. (1982) Buffers of constant ionic strength for studying pH-dependent processes. Methods Enzymol. 87C, 405-426
    • (1982) Methods Enzymol. , vol.87 C , pp. 405-426
    • Ellis, K.J.1    Morrison, J.F.2
  • 33
    • 0033544694 scopus 로고    scopus 로고
    • Calcium-mediated thermostability in the subtilisin superfamily: The crystal structure of Bacillus Ak.1 protease at 1.8 angstrom resolution
    • Smith, C. A., Toogood, H. S., Baker, H. M., Daniel, R. M. and Baker, E. N. (1999) Calcium-mediated thermostability in the subtilisin superfamily: the crystal structure of Bacillus Ak.1 protease at 1.8 angstrom resolution. J. Mol. Biol. 294, 1027-1040
    • (1999) J. Mol. Biol. , vol.294 , pp. 1027-1040
    • Smith, C.A.1    Toogood, H.S.2    Baker, H.M.3    Daniel, R.M.4    Baker, E.N.5
  • 34
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I. and Berger, A. (1967) On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 127, 157-162
    • (1967) Biochem. Biophys. Res. Commun. , vol.127 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 35
    • 0026638586 scopus 로고
    • Extensive comparison of the substrate preferences of two subtilisins as determined with peptide substrates which are based on the principle of intramolecular quenching
    • Grøn, H., Meldal, M. and Breddam, K. (1992) Extensive comparison of the substrate preferences of two subtilisins as determined with peptide substrates which are based on the principle of intramolecular quenching. Biochemistry 31, 6011-6018
    • (1992) Biochemistry , vol.31 , pp. 6011-6018
    • Grøn, H.1    Meldal, M.2    Breddam, K.3
  • 36
    • 0034101067 scopus 로고    scopus 로고
    • Purification and characterization of hordolisin, a subtilisin-like serine endoprotease from barley
    • Terp, N., Thomsen, K. K., Svendsen, I., Davy, A. and Simpson, D. J. (2000) Purification and characterization of hordolisin, a subtilisin-like serine endoprotease from barley. J. Plant Physiol. 156, 468-476
    • (2000) J. Plant Physiol. , vol.156 , pp. 468-476
    • Terp, N.1    Thomsen, K.K.2    Svendsen, I.3    Davy, A.4    Simpson, D.J.5
  • 37
    • 0034681401 scopus 로고    scopus 로고
    • LeSBT1, a subtilase from tomato plants - Overexpression in insect cells, purification and characterization
    • Janzik, I., Macheroux, P., Amrhein, N. and Schaller, A. (2000) LeSBT1, a subtilase from tomato plants - overexpression in insect cells, purification and characterization. J. Biol. Chem. 275, 5193-5199
    • (2000) J. Biol. Chem. , vol.275 , pp. 5193-5199
    • Janzik, I.1    Macheroux, P.2    Amrhein, N.3    Schaller, A.4
  • 38
    • 0343517090 scopus 로고    scopus 로고
    • Cleavage specificity of cucumisin, a serine protease, with synthetic substrates
    • Arima, K., Yonezawa, H., Uchikoba, T., Shimada, M. and Kaneda, M. (2000) Cleavage specificity of cucumisin, a serine protease, with synthetic substrates. Phytochemistry 54, 451-454
    • (2000) Phytochemistry , vol.54 , pp. 451-454
    • Arima, K.1    Yonezawa, H.2    Uchikoba, T.3    Shimada, M.4    Kaneda, M.5
  • 39
    • 0030911517 scopus 로고    scopus 로고
    • Cleavage site for sterol-regulated protease localized to a Leu-Ser bond in the lumenal loop of sterol regulatory element-binding protein-2
    • Duncan, E. A., Brown, M. S., Goldstein, J. L. and Sakai, J. (1997) Cleavage site for sterol-regulated protease localized to a Leu-Ser bond in the lumenal loop of sterol regulatory element-binding protein-2. J. Biol. Chem. 272, 12778-12785
    • (1997) J. Biol. Chem. , vol.272 , pp. 12778-12785
    • Duncan, E.A.1    Brown, M.S.2    Goldstein, J.L.3    Sakai, J.4
  • 40
    • 0026911103 scopus 로고
    • The Acid Growth Theory of auxin-induced cell elongation is alive and well
    • Rayle, D. L. and Cleland, R. E. (1992) The Acid Growth Theory of auxin-induced cell elongation is alive and well. Plant Physiol. 99, 1271-1274
    • (1992) Plant Physiol. , vol.99 , pp. 1271-1274
    • Rayle, D.L.1    Cleland, R.E.2
  • 41
    • 0031704475 scopus 로고    scopus 로고
    • Localized changes in apoplastic and cytoplasmic pH are associated with root hair development in Arabidopsis thaliana
    • Bibikova, T. N., Jacob, T., Dahse, I. and Gilroy, S. (1998) Localized changes in apoplastic and cytoplasmic pH are associated with root hair development in Arabidopsis thaliana. Development 125, 2925-2934
    • (1998) Development , vol.125 , pp. 2925-2934
    • Bibikova, T.N.1    Jacob, T.2    Dahse, I.3    Gilroy, S.4
  • 43
    • 0035142574 scopus 로고    scopus 로고
    • Polypeptide hormones
    • Ryan, C. A. and Pearce, G. (2001) Polypeptide hormones. Plant Physiol. 125, 65-68
    • (2001) Plant Physiol. , vol.125 , pp. 65-68
    • Ryan, C.A.1    Pearce, G.2
  • 44
    • 0032902612 scopus 로고    scopus 로고
    • Naturiuretic peptides - A new class of plant hormone?
    • Gehring, C. A. (1999) Naturiuretic peptides - a new class of plant hormone? Ann. Bot. 83, 329-334
    • (1999) Ann. Bot. , vol.83 , pp. 329-334
    • Gehring, C.A.1
  • 45
    • 0026545605 scopus 로고
    • Structure, expression and antisense inhibition of the systemin precursor gene
    • McGurl, B., Pearce, G., Orozco-Cardenas, M. and Ryan, C. A. (1992) Structure, expression and antisense inhibition of the systemin precursor gene. Science 255, 1570-1573
    • (1992) Science , vol.255 , pp. 1570-1573
    • McGurl, B.1    Pearce, G.2    Orozco-Cardenas, M.3    Ryan, C.A.4
  • 46
    • 0033583173 scopus 로고    scopus 로고
    • Signalling of cell fate decisions by CLAVATA3 in Arabidopsis shoot meristems
    • Fletcher, J. C., Brand, U., Running, M. P., Simon, R. and Meyerowitz, E. M. (1999) Signalling of cell fate decisions by CLAVATA3 in Arabidopsis shoot meristems. Science 283, 1911-1914
    • (1999) Science , vol.283 , pp. 1911-1914
    • Fletcher, J.C.1    Brand, U.2    Running, M.P.3    Simon, R.4    Meyerowitz, E.M.5
  • 47
    • 0029084061 scopus 로고
    • The extracellular matrix in higher plants. 4. Developmentally regulated proteoglycans and glycoproteins of the plant cell surface
    • Knox, J. P. (1995) The extracellular matrix in higher plants. 4. Developmentally regulated proteoglycans and glycoproteins of the plant cell surface. FASEB J. 9, 1004-1012
    • (1995) FASEB J. , vol.9 , pp. 1004-1012
    • Knox, J.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.