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Volumn 169, Issue 4, 2005, Pages 776-784

Isolation and expression of protein disulfide isomerase cDNA from sweet potato (Ipomoea batatas [L.] Lam 'Tainong 57') storage roots

Author keywords

cDNA sequence; Dehydroascorbate; Expression; Monodehydroascorbate; Protein disulfide isomerase; Sweet potato

Indexed keywords

AMINO ACIDS; ANTIOXIDANTS; CLONING; ENZYMES; PLANTS (BOTANY); RNA;

EID: 23244451433     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2005.05.034     Document Type: Article
Times cited : (27)

References (43)
  • 1
    • 0026731788 scopus 로고
    • Protein disulfide isomerase: A multifunctional protein resident in the lumen of the endoplasmic reticulum
    • R. Noiva, and W.J. Lennarz Protein disulfide isomerase: a multifunctional protein resident in the lumen of the endoplasmic reticulum J. Biol. Chem. 267 1992 3553 3556
    • (1992) J. Biol. Chem. , vol.267 , pp. 3553-3556
    • Noiva, R.1    Lennarz, W.J.2
  • 2
    • 0024337857 scopus 로고
    • Protein disulfide isomerase: Multiple roles in modification of nascent secretory proteins
    • R.B. Freedman Protein disulfide isomerase: multiple roles in modification of nascent secretory proteins Cell 57 1989 1069 1072
    • (1989) Cell , vol.57 , pp. 1069-1072
    • Freedman, R.B.1
  • 3
    • 0023303619 scopus 로고
    • Molecular cloning of the β-subunit of human prolyl 4-hydroxylase. This subunit and protein disulfide isomerase are products of same gene
    • T. Pihlajaniemi, T. Helaakoski, K. Tasanen, R. Myllylä, M.-L. Huhtala, J. Koivu, and K.I. Kivirikko Molecular cloning of the β-subunit of human prolyl 4-hydroxylase. This subunit and protein disulfide isomerase are products of same gene EMBO J. 6 1987 643 649
    • (1987) EMBO J. , vol.6 , pp. 643-649
    • Pihlajaniemi, T.1    Helaakoski, T.2    Tasanen, K.3    Myllylä, R.4    Huhtala, M.-L.5    Koivu, J.6    Kivirikko, K.I.7
  • 4
    • 0025082330 scopus 로고
    • Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity
    • W.W. Wells, D.P. Xu, Y. Yang, and P.A. Rocque Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity J. Biol. Chem. 265 1990 15361 15364
    • (1990) J. Biol. Chem. , vol.265 , pp. 15361-15364
    • Wells, W.W.1    Xu, D.P.2    Yang, Y.3    Rocque, P.A.4
  • 5
    • 0025855390 scopus 로고
    • Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast
    • M. Lamantia, T. Miura, H. Tachikawa, H.A. Kaplan, W.J. Lennarz, and T. Mizunaga Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast Proc. Natl. Acad. Sci. U.S.A. 88 1991 4453 4457
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 4453-4457
    • Lamantia, M.1    Miura, T.2    Tachikawa, H.3    Kaplan, H.A.4    Lennarz, W.J.5    Mizunaga, T.6
  • 6
    • 0025329901 scopus 로고
    • Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex
    • J.R. Wetterau, K.A. Combs, S.N. Spinner, and B.G. Joiner Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex J. Biol. Chem. 265 1990 9800 9807
    • (1990) J. Biol. Chem. , vol.265 , pp. 9800-9807
    • Wetterau, J.R.1    Combs, K.A.2    Spinner, S.N.3    Joiner, B.G.4
  • 7
    • 0023687758 scopus 로고
    • Molecular cloning and complete amino-acid sequence of form-I phosphoinositide specific phospholipase C
    • C.F. Bennett, J.M. Balcarek, A. Varricho, and S.T. Crooke Molecular cloning and complete amino-acid sequence of form-I phosphoinositide specific phospholipase C Nature 334 1988 268 270
    • (1988) Nature , vol.334 , pp. 268-270
    • Bennett, C.F.1    Balcarek, J.M.2    Varricho, A.3    Crooke, S.T.4
  • 8
    • 0032540349 scopus 로고    scopus 로고
    • ERcalcistorin/protein disulfide-isomerase acts as a calcium storage protein in the endoplasmic reticulum of a living cell
    • H.A. Lucero, D. Lebeche, and B. Kaminer ERcalcistorin/protein disulfide-isomerase acts as a calcium storage protein in the endoplasmic reticulum of a living cell J. Biol. Chem. 273 1998 9857 9863
    • (1998) J. Biol. Chem. , vol.273 , pp. 9857-9863
    • Lucero, H.A.1    Lebeche, D.2    Kaminer, B.3
  • 9
    • 0023182842 scopus 로고
    • The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum
    • S.-Y. Cheng, Q.-H. Gong, C. Parkison, E.A. Robinson, E. Appella, G.T. Merlino, and I. Pastan The nucleotide sequence of a human cellular thyroid hormone binding protein present in endoplasmic reticulum J. Biol. Chem. 262 1987 11221 11227
    • (1987) J. Biol. Chem. , vol.262 , pp. 11221-11227
    • Cheng, S.-Y.1    Gong, Q.-H.2    Parkison, C.3    Robinson, E.A.4    Appella, E.5    Merlino, G.T.6    Pastan, I.7
  • 10
    • 0026523624 scopus 로고
    • Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope
    • J. Denecke, R.D. Rycke, and J. Botterman Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope EMBO J. 11 1992 2345 2355
    • (1992) EMBO J. , vol.11 , pp. 2345-2355
    • Denecke, J.1    Rycke, R.D.2    Botterman, J.3
  • 11
    • 0032540353 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen
    • R. Wilson, J.F. Lees, and N.J. Bulleid Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen J. Biol. Chem. 273 1998 9637 9643
    • (1998) J. Biol. Chem. , vol.273 , pp. 9637-9643
    • Wilson, R.1    Lees, J.F.2    Bulleid, N.J.3
  • 12
    • 0032478663 scopus 로고    scopus 로고
    • Enzymes as chaperones and chaperones as enzymes
    • C.C. Wang, and C.L. Tsou Enzymes as chaperones and chaperones as enzymes FEBS Lett. 425 1998 382 384
    • (1998) FEBS Lett. , vol.425 , pp. 382-384
    • Wang, C.C.1    Tsou, C.L.2
  • 13
    • 0025840492 scopus 로고
    • Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase
    • B.S. Shorrosh, and R.A. Dixon Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase Proc. Natl. Acad. Sci. U.S.A. 88 1991 10941 10945
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10941-10945
    • Shorrosh, B.S.1    Dixon, R.A.2
  • 14
    • 0026617677 scopus 로고
    • Molecular characterization and expression of an alfalfa protein with sequence similarity to mammalian ERp72, a glucose-regulated endoplasmic reticulum protein containing active site sequences of protein disulphide isomerase
    • B.S. Shorrosh, and R.A. Dixon Molecular characterization and expression of an alfalfa protein with sequence similarity to mammalian ERp72, a glucose-regulated endoplasmic reticulum protein containing active site sequences of protein disulphide isomerase Plant J. 2 1992 51 58
    • (1992) Plant J. , vol.2 , pp. 51-58
    • Shorrosh, B.S.1    Dixon, R.A.2
  • 15
    • 0028726236 scopus 로고
    • Nucleotide sequence and developmental expression of duplicated genes encoding protein disulfide isomerase in barley (Hordeum vulgare L.)
    • F. Chen, and P.M. Hayes Nucleotide sequence and developmental expression of duplicated genes encoding protein disulfide isomerase in barley (Hordeum vulgare L.) Plant Physiol. 106 1994 1705 1706
    • (1994) Plant Physiol. , vol.106 , pp. 1705-1706
    • Chen, F.1    Hayes, P.M.2
  • 16
    • 0029206643 scopus 로고
    • Nucleotide sequence of a wheat cDNA encoding protein disulfide isomerase
    • Y. Shimoni, G. Segal, X. Zhu, and G. Galili Nucleotide sequence of a wheat cDNA encoding protein disulfide isomerase Plant Physiol. 107 1995 281
    • (1995) Plant Physiol. , vol.107 , pp. 281
    • Shimoni, Y.1    Segal, G.2    Zhu, X.3    Galili, G.4
  • 17
    • 0030099075 scopus 로고    scopus 로고
    • Expression of protein disulfide isomerase is elevated in the endosperm of the maize floury-2 mutant
    • C.P. Li, and B.A. Larkins Expression of protein disulfide isomerase is elevated in the endosperm of the maize floury-2 mutant Plant Mol. Biol. 30 1996 873 882
    • (1996) Plant Mol. Biol. , vol.30 , pp. 873-882
    • Li, C.P.1    Larkins, B.A.2
  • 18
    • 0030042362 scopus 로고    scopus 로고
    • Molecular characterization of plant endoplasmic reticulum: Identification of protein disulfide isomerase as the major reticuloplasmin
    • S.J. Coughlan, C. Hastings, and R.J. Winfrey Molecular characterization of plant endoplasmic reticulum: identification of protein disulfide isomerase as the major reticuloplasmin Eur. J. Biochem. 235 1996 215 224
    • (1996) Eur. J. Biochem. , vol.235 , pp. 215-224
    • Coughlan, S.J.1    Hastings, C.2    Winfrey, R.J.3
  • 20
    • 0027968068 scopus 로고
    • Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position- specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, T.J. Gibson, and W. Clustal Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position- specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3    Clustal, W.4
  • 21
    • 1242300085 scopus 로고    scopus 로고
    • Isolation and characterization of thioredoxin h cDNA from sweet potato (Ipomoea batatas [L.] Lam 'Tainong 57') storage roots
    • D.J. Huang, H.J. Chen, W.C. Hou, and Y.H. Lin Isolation and characterization of thioredoxin h cDNA from sweet potato (Ipomoea batatas [L.] Lam 'Tainong 57') storage roots Plant Sci. 166 2004 515 523
    • (2004) Plant Sci. , vol.166 , pp. 515-523
    • Huang, D.J.1    Chen, H.J.2    Hou, W.C.3    Lin, Y.H.4
  • 22
    • 1242277736 scopus 로고    scopus 로고
    • In vitro reduction of trypsin inhibitor by purified NADPH/ Thioredoxin system from sprouts of sweet potato (Ipomoea batatas (L) Lam.) storage roots
    • D.J. Huang, H.J. Chen, W.C. Hou, T.E. Chen, and Y.H. Lin In vitro reduction of trypsin inhibitor by purified NADPH/ Thioredoxin system from sprouts of sweet potato (Ipomoea batatas (L) Lam.) storage roots Plant Sci. 166 2004 435 441
    • (2004) Plant Sci. , vol.166 , pp. 435-441
    • Huang, D.J.1    Chen, H.J.2    Hou, W.C.3    Chen, T.E.4    Lin, Y.H.5
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 885
    • (1970) Nature , vol.227 , pp. 680-885
    • Laemmli, U.K.1
  • 24
    • 0020787907 scopus 로고
    • Kinetics and specificity of homogeneous protein disulfide-isomerase in protein disulfide isomerization and thiol-protein-disulfide oxidoreduction
    • N. Lambert, and R.B. Freedman Kinetics and specificity of homogeneous protein disulfide-isomerase in protein disulfide isomerization and thiol-protein-disulfide oxidoreduction Biochem. J. 213 1983 235 243
    • (1983) Biochem. J. , vol.213 , pp. 235-243
    • Lambert, N.1    Freedman, R.B.2
  • 25
    • 0030755059 scopus 로고    scopus 로고
    • Dehydroascorbate reductase and monodehydroascorbate reductase activities of trypsin inhibitors, the major sweet potato (Ipomoea batatas [L.] Lam) root storage protein
    • W.C. Hou, and Y.H. Lin Dehydroascorbate reductase and monodehydroascorbate reductase activities of trypsin inhibitors, the major sweet potato (Ipomoea batatas [L.] Lam) root storage protein Plant Sci. 128 1997 151 158
    • (1997) Plant Sci. , vol.128 , pp. 151-158
    • Hou, W.C.1    Lin, Y.H.2
  • 26
    • 0002977651 scopus 로고
    • Mechanism of free radical formation and disappearance during the ascorbic acid oxidase and peroxidase reactions
    • I. Yamazaki, and L.H. Pette Mechanism of free radical formation and disappearance during the ascorbic acid oxidase and peroxidase reactions Biochem. Biophys. Acta 50 1961 62 69
    • (1961) Biochem. Biophys. Acta , vol.50 , pp. 62-69
    • Yamazaki, I.1    Pette, L.H.2
  • 27
    • 0022387362 scopus 로고
    • Sequence of protein disulfide isomerase and implications of its relationship to thioredoxin
    • J.C. Edman, L. Ellis, R.W. Blacher, R.A. Roth, and W.J. Rutter Sequence of protein disulfide isomerase and implications of its relationship to thioredoxin Nature 317 1985 267 270
    • (1985) Nature , vol.317 , pp. 267-270
    • Edman, J.C.1    Ellis, L.2    Blacher, R.W.3    Roth, R.A.4    Rutter, W.J.5
  • 28
    • 0026705344 scopus 로고
    • Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli
    • K. Vuori, R. Myllylä, T. Pihlajaniemi, and K.I. Kivirikko Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli J. Biol. Chem. 267 1992 7211 7214
    • (1992) J. Biol. Chem. , vol.267 , pp. 7211-7214
    • Vuori, K.1    Myllylä, R.2    Pihlajaniemi, T.3    Kivirikko, K.I.4
  • 29
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal-sequence cleavage sites
    • G. Von Heijne Patterns of amino acids near signal-sequence cleavage sites Eur. J. Biochem. 133 1983 17 21
    • (1983) Eur. J. Biochem. , vol.133 , pp. 17-21
    • Von Heijne, G.1
  • 30
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • H. Nielsen, J. Engelbrecht, S. Brunak, and G. von Heijne Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites Protein Eng. 10 1997 1 6
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 31
    • 0026523624 scopus 로고
    • Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope
    • J. Denecke, R.D. Rycke, and J. Botterman Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope EMBO J. 11 1992 2345 2355
    • (1992) EMBO J. , vol.11 , pp. 2345-2355
    • Denecke, J.1    Rycke, R.D.2    Botterman, J.3
  • 32
    • 0025367812 scopus 로고
    • Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: Implications for protein engineering
    • Y. Gavel, and G. von Heijne Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering Protein Eng. 3 1990 433 442
    • (1990) Protein Eng. , vol.3 , pp. 433-442
    • Gavel, Y.1    Von Heijne, G.2
  • 33
    • 0030099075 scopus 로고    scopus 로고
    • Expression of protein disulfide isomerase is elevated in the endosperm of the maize floury-2 mutant
    • C.-P. Li, and B.A. Larkins Expression of protein disulfide isomerase is elevated in the endosperm of the maize floury-2 mutant Plant Mol. Biol. 30 1996 873 882
    • (1996) Plant Mol. Biol. , vol.30 , pp. 873-882
    • Li, C.-P.1    Larkins, B.A.2
  • 34
    • 0025840492 scopus 로고
    • Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C
    • B.S. Shorrosh, and R.A. Dixon Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C Proc. Natl. Acad. Sci. U.S.A. 88 1991 10941 10945
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10941-10945
    • Shorrosh, B.S.1    Dixon, R.A.2
  • 35
    • 0001864819 scopus 로고
    • Tissue-specific expression of cell wall proteins in developing soybean tissues
    • Z.H. Ye, and J.E. Varner Tissue-specific expression of cell wall proteins in developing soybean tissues Plant Cell 3 1991 23 37
    • (1991) Plant Cell , vol.3 , pp. 23-37
    • Ye, Z.H.1    Varner, J.E.2
  • 36
    • 2442761708 scopus 로고    scopus 로고
    • The protein disulphide-isomerase family: Unravelling a string of folds
    • D.M. Ferrari, and H.D. Söling The protein disulphide-isomerase family: unravelling a string of folds Biochem. J. 339 1999 1 10
    • (1999) Biochem. J. , vol.339 , pp. 1-10
    • Ferrari, D.M.1    Söling, H.D.2
  • 37
    • 0013838236 scopus 로고
    • Enzymatically catalyzed disulfide interchange in randomly crosslinked soybean trypsin inhibitor
    • R.F. Steiner, F.D. Lorenzo, and C.B. Anfinsen Enzymatically catalyzed disulfide interchange in randomly crosslinked soybean trypsin inhibitor J. Biol. Chem. 240 1965 4648 4651
    • (1965) J. Biol. Chem. , vol.240 , pp. 4648-4651
    • Steiner, R.F.1    Lorenzo, F.D.2    Anfinsen, C.B.3
  • 38
    • 0037028507 scopus 로고    scopus 로고
    • Molecular characterization of a novel protein disulfide isomerase in carrot
    • Z.J. Xu, K. Ueda, K. Masuda, M. Ono, and M. Inoue Molecular characterization of a novel protein disulfide isomerase in carrot Gene 284 2002 225 231
    • (2002) Gene , vol.284 , pp. 225-231
    • Xu, Z.J.1    Ueda, K.2    Masuda, K.3    Ono, M.4    Inoue, M.5
  • 39
    • 0025840492 scopus 로고
    • Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C
    • B.S. Shorrosh, and R.A. Dixon Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C Proc. Natl. Acad. Sci. U.S.A. 88 1991 10941 10945
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10941-10945
    • Shorrosh, B.S.1    Dixon, R.A.2
  • 40
    • 0025082330 scopus 로고
    • Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity
    • W.W. Wells, D.P. Wu, Y. Yang, and P.A. Rocque Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity J. Biol. Chem. 265 1990 15361 15364
    • (1990) J. Biol. Chem. , vol.265 , pp. 15361-15364
    • Wells, W.W.1    Wu, D.P.2    Yang, Y.3    Rocque, P.A.4
  • 42
    • 0002977651 scopus 로고
    • Mechanism of free radical formation and disappearance during the ascorbic acid oxidase and peroxidase reactions
    • I. Yamazaki, and L.H. Pette Mechanism of free radical formation and disappearance during the ascorbic acid oxidase and peroxidase reactions Biochem. Biophys. Acta 50 1961 62 69
    • (1961) Biochem. Biophys. Acta , vol.50 , pp. 62-69
    • Yamazaki, I.1    Pette, L.H.2
  • 43
    • 0000918942 scopus 로고
    • Monodehydroascorbate reductase in spinach chloroplasts and its participation in regeneration of ascorbate for scavenging hydrogen peroxide
    • M.A. Hossain, Y. Nakano, and K. Asada Monodehydroascorbate reductase in spinach chloroplasts and its participation in regeneration of ascorbate for scavenging hydrogen peroxide Plant Cell Physiol. 25 1984 385 395
    • (1984) Plant Cell Physiol. , vol.25 , pp. 385-395
    • Hossain, M.A.1    Nakano, Y.2    Asada, K.3


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