메뉴 건너뛰기




Volumn 72, Issue 4, 2006, Pages 238-246

A pea NTPase, PsAPY1, recognizes signal molecules from microorganisms

Author keywords

Binding protein; Cell wall; Elicitor; NTPase; Receptor; Suppressor of defense

Indexed keywords

BACTERIA (MICROORGANISMS); DIDYMELLA PINODES; ESCHERICHIA COLI; PISUM SATIVUM;

EID: 33748098340     PISSN: 13452630     EISSN: 1610739X     Source Type: Journal    
DOI: 10.1007/s10327-006-0279-7     Document Type: Article
Times cited : (14)

References (55)
  • 1
    • 0026675220 scopus 로고
    • Elicitors and suppressors of the defense response in tomato cells. Purification and characterization of glycopeptide elicitors and glycan suppressors generated by enzymatic cleavage of yeast invertase
    • CW Basse K Bock T Boller 1992 Elicitors and suppressors of the defense response in tomato cells. Purification and characterization of glycopeptide elicitors and glycan suppressors generated by enzymatic cleavage of yeast invertase J Biol Chem 267 10258 10265
    • (1992) J Biol Chem , vol.267 , pp. 10258-10265
    • Basse, C.W.1    Bock, K.2    Boller, T.3
  • 2
    • 0027197331 scopus 로고
    • High affinity binding of glycopeptide elicitor to tomato cells and microsomal membranes and displacement by specific glycan
    • CW Basse A Fath T Boller 1993 High affinity binding of glycopeptide elicitor to tomato cells and microsomal membranes and displacement by specific glycan J Biol Chem 268 14724 14731
    • (1993) J Biol Chem , vol.268 , pp. 14724-14731
    • Basse, C.W.1    Fath, A.2    Boller, T.3
  • 3
    • 0034705522 scopus 로고    scopus 로고
    • First apyrase splice variants have different enzymatic properties
    • A Biederbick C Kosan J Kunz HP Elsasser 2000 First apyrase splice variants have different enzymatic properties J Biol Chem 275 19018 19024
    • (2000) J Biol Chem , vol.275 , pp. 19018-19024
    • Biederbick, A.1    Kosan, C.2    Kunz, J.3    Elsasser, H.P.4
  • 4
    • 0028797143 scopus 로고
    • Chemoperception of microbial signals in plant cells
    • T Boller 1995 Chemoperception of microbial signals in plant cells Annu Rev Plant Physiol Plant Mol Biol 46 189 214
    • (1995) Annu Rev Plant Physiol Plant Mol Biol , vol.46 , pp. 189-214
    • Boller, T.1
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • MM Bradford 1976 A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal Biochem 72 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0026735576 scopus 로고
    • Elicitor- and wound-induced oxidative cross-linking of a proline-rich plant cell wall protein: A novel rapid defense response
    • D Bradly P Kjellbom CJ Lamb 1992 Elicitor- and wound-induced oxidative cross-linking of a proline-rich plant cell wall protein: a novel rapid defense response Cell 70 21 30
    • (1992) Cell , vol.70 , pp. 21-30
    • Bradly, D.1    Kjellbom, P.2    Lamb, C.J.3
  • 7
    • 0028191619 scopus 로고
    • Function of oxidative cross-linking of cell wall structural proteins in plant disease resistance
    • LF Brisson R Tenhaken CJ Lamb 1994 Function of oxidative cross-linking of cell wall structural proteins in plant disease resistance Plant Cell 6 1703 1712
    • (1994) Plant Cell , vol.6 , pp. 1703-1712
    • Brisson, L.F.1    Tenhaken, R.2    Lamb, C.J.3
  • 8
    • 0023039744 scopus 로고
    • Characterization of nucleoside triphosphatase activity in isolated pea nuclei and its photoreversible regulation by light
    • YR Chen SJ Roux 1986 Characterization of nucleoside triphosphatase activity in isolated pea nuclei and its photoreversible regulation by light Plant Physiol 81 609 613
    • (1986) Plant Physiol , vol.81 , pp. 609-613
    • Chen, Y.R.1    Roux, S.J.2
  • 9
    • 0027771221 scopus 로고
    • Solubilization of functional plasma membrane-localized hepta-β-glucoside elicitor-binding proteins from soybean
    • JJ Cheong R Alba F Cote J Enkerli MG Hahn 1993 Solubilization of functional plasma membrane-localized hepta-β-glucoside elicitor-binding proteins from soybean Plant Physiol 103 1173 1182
    • (1993) Plant Physiol , vol.103 , pp. 1173-1182
    • Cheong, J.J.1    Alba, R.2    Cote, F.3    Enkerli, J.4    Hahn, M.G.5
  • 10
    • 0024059214 scopus 로고
    • High-affinity binding of fungal β-glucan fragments to soybean (Glycine max L.) microsomal fractions and protoplasts
    • EG Cosio H Popperl WE Schmidt J Ebel 1988 High-affinity binding of fungal β-glucan fragments to soybean (Glycine max L.) microsomal fractions and protoplasts Eur J Biochem 175 309 315
    • (1988) Eur J Biochem , vol.175 , pp. 309-315
    • Cosio, E.G.1    Popperl, H.2    Schmidt, W.E.3    Ebel, J.4
  • 15
    • 0000230697 scopus 로고
    • Host-pathogen interactions. XIX. the endogenous elicitor, a fragment of a plant cell wall polysaccharide that elicits phytoalexin accumulation in soybeans
    • MG Hahn AG Darvill P Albersheim 1981 Host-pathogen interactions. XIX. The endogenous elicitor, a fragment of a plant cell wall polysaccharide that elicits phytoalexin accumulation in soybeans Plant Physiol 68 1161 1169
    • (1981) Plant Physiol , vol.68 , pp. 1161-1169
    • Hahn, M.G.1    Darvill, A.G.2    Albersheim, P.3
  • 16
    • 0030034867 scopus 로고    scopus 로고
    • Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum)
    • M Handa G Guidotti 1996 Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum) Biochem Biophys Res Commun 218 916 923
    • (1996) Biochem Biophys Res Commun , vol.218 , pp. 916-923
    • Handa, M.1    Guidotti, G.2
  • 18
    • 0030019538 scopus 로고    scopus 로고
    • Light modulated abundance of an mRNA encoding a calmodulin-regulated, chromatin-associated NTPase in pea
    • HL Hsieh CG Tong C Thomas SJ Roux 1996 Light modulated abundance of an mRNA encoding a calmodulin-regulated, chromatin-associated NTPase in pea Plant Mol Biol 30 135 147
    • (1996) Plant Mol Biol , vol.30 , pp. 135-147
    • Hsieh, H.L.1    Tong, C.G.2    Thomas, C.3    Roux, S.J.4
  • 19
    • 0031213917 scopus 로고    scopus 로고
    • Identification of a high-affinity binding protein for N-acetylchitooligosaccharide elicitor in the plasma membrane of suspension cultured rice cells by affinity labeling
    • Y Ito H Kaku N Shibuya 1997 Identification of a high-affinity binding protein for N-acetylchitooligosaccharide elicitor in the plasma membrane of suspension cultured rice cells by affinity labeling Plant J 12 347 356
    • (1997) Plant J , vol.12 , pp. 347-356
    • Ito, Y.1    Kaku, H.2    Shibuya, N.3
  • 20
    • 16644366421 scopus 로고    scopus 로고
    • Evidence of novel cell signaling role for extracellular adenosine triphosphates and diphosphates in Arabidopsis
    • CR Jeter W Tang E Henaff T Butterfield SJ Roux 2004 Evidence of novel cell signaling role for extracellular adenosine triphosphates and diphosphates in Arabidopsis Plant Cell 16 2652 2664
    • (2004) Plant Cell , vol.16 , pp. 2652-2664
    • Jeter, C.R.1    Tang, W.2    Henaff, E.3    Butterfield, T.4    Roux, S.J.5
  • 23
    • 0028814110 scopus 로고
    • Specific inhibition of cell wall-bound ATPase by fungal suppressor from Mycosphaerella pinodes
    • A Kiba K Toyoda T Yamada Y Ichinose T Shiraishi 1995 Specific inhibition of cell wall-bound ATPase by fungal suppressor from Mycosphaerella pinodes Plant Cell Physiol 36 809 817
    • (1995) Plant Cell Physiol , vol.36 , pp. 809-817
    • Kiba, A.1    Toyoda, K.2    Yamada, T.3    Ichinose, Y.4    Shiraishi, T.5
  • 24
    • 0000396838 scopus 로고    scopus 로고
    • Specific response of partially purified cell wall-bound ATPase to fungal suppressor
    • A Kiba K Toyoda Y Ichinose T Yamada T Shiraishi 1996 Specific response of partially purified cell wall-bound ATPase to fungal suppressor Plant Cell Physiol 37 207 214
    • (1996) Plant Cell Physiol , vol.37 , pp. 207-214
    • Kiba, A.1    Toyoda, K.2    Ichinose, Y.3    Yamada, T.4    Shiraishi, T.5
  • 25
    • 0030824754 scopus 로고    scopus 로고
    • Superoxide generation in extracts from isolated plant cell wall is regulated by fungal signal molecules
    • A Kiba C Miyake K Toyoda Y Ichinose T Yamada T Shiraishi 1997 Superoxide generation in extracts from isolated plant cell wall is regulated by fungal signal molecules Phytopathology 87 846 852
    • (1997) Phytopathology , vol.87 , pp. 846-852
    • Kiba, A.1    Miyake, C.2    Toyoda, K.3    Ichinose, Y.4    Yamada, T.5    Shiraishi, T.6
  • 26
    • 0033198624 scopus 로고    scopus 로고
    • Induction of defense responses by synthetic glycopeptides that have partial structure of the elicitor from Mycosphaerella pinodes
    • A Kiba K Toyoda T Yamada Y Ichinose T Shiraishi 1999 Induction of defense responses by synthetic glycopeptides that have partial structure of the elicitor from Mycosphaerella pinodes Plant Cell Physiol 40 978 985
    • (1999) Plant Cell Physiol , vol.40 , pp. 978-985
    • Kiba, A.1    Toyoda, K.2    Yamada, T.3    Ichinose, Y.4    Shiraishi, T.5
  • 28
    • 0023157708 scopus 로고
    • The structure and physiological activity of glycoprotein secreted from conidia of Mycosphaerella pinodes II
    • M Matsubara H Kuroda 1987 The structure and physiological activity of glycoprotein secreted from conidia of Mycosphaerella pinodes II Chem Pharm Bull 35 249 255
    • (1987) Chem Pharm Bull , vol.35 , pp. 249-255
    • Matsubara, M.1    Kuroda, H.2
  • 30
    • 0025933503 scopus 로고
    • Expert system for prediction protein localization sites in gram-negative bacteria
    • K Nakai M Kanehisa 1991 Expert system for prediction protein localization sites in gram-negative bacteria Proteins 11 95 110
    • (1991) Proteins , vol.11 , pp. 95-110
    • Nakai, K.1    Kanehisa, M.2
  • 31
    • 0033136084 scopus 로고    scopus 로고
    • Non-invasive quantitative detection and applications of non-toxic, S65T-type green fluorescent protein in living plants
    • Y Niwa T Hirano K Yoshimoto M Shimizu H Kobayashi 1999 Non-invasive quantitative detection and applications of non-toxic, S65T-type green fluorescent protein in living plants Plant J 18 455 463
    • (1999) Plant J , vol.18 , pp. 455-463
    • Niwa, Y.1    Hirano, T.2    Yoshimoto, K.3    Shimizu, M.4    Kobayashi, H.5
  • 32
    • 0027967403 scopus 로고
    • High affinity binding of a fungal oligopeptide elicitor to parsley plasma membranes triggers multiple defense responses
    • T Nurnberger D Nennstiel T Jabs WR Sacks K Hahlbrock D Scheel 1994 High affinity binding of a fungal oligopeptide elicitor to parsley plasma membranes triggers multiple defense responses Cell 78 449 460
    • (1994) Cell , vol.78 , pp. 449-460
    • Nurnberger, T.1    Nennstiel, D.2    Jabs, T.3    Sacks, W.R.4    Hahlbrock, K.5    Scheel, D.6
  • 33
    • 0028920243 scopus 로고
    • Covalent cross-linking of the Phytophthora megasperma oligopeptide elicitor to its receptor in parsley membrane
    • T Nurnberger D Nennstiel K Hahlbrock D Scheel 1995 Covalent cross-linking of the Phytophthora megasperma oligopeptide elicitor to its receptor in parsley membrane Proc Natl Acad Sci USA 90 2338 2342
    • (1995) Proc Natl Acad Sci USA , vol.90 , pp. 2338-2342
    • Nurnberger, T.1    Nennstiel, D.2    Hahlbrock, K.3    Scheel, D.4
  • 34
    • 0001411580 scopus 로고
    • Characterization of ATPase activity associated with corn leaf plasma membrane
    • DS Perlin RM Spanswick 1981 Characterization of ATPase activity associated with corn leaf plasma membrane Plant Physiol 68 521 526
    • (1981) Plant Physiol , vol.68 , pp. 521-526
    • Perlin, D.S.1    Spanswick, R.M.2
  • 35
    • 0028967657 scopus 로고
    • Ecto-ATPase: Identities and functions
    • L Plesner 1995 Ecto-ATPase: identities and functions Int Rev Cytol 158 141 214
    • (1995) Int Rev Cytol , vol.158 , pp. 141-214
    • Plesner, L.1
  • 36
    • 0031754497 scopus 로고    scopus 로고
    • Receptors for purines and pyrimidines
    • V Ralevic G Burnstock 1998 Receptors for purines and pyrimidines Pharmacol Rev 50 413 492
    • (1998) Pharmacol Rev , vol.50 , pp. 413-492
    • Ralevic, V.1    Burnstock, G.2
  • 37
    • 0035083333 scopus 로고    scopus 로고
    • Structure of the coding region and mRNA variants of the apyrase gene from pea (Pisum sativum)
    • K Shibata S Abe E Davies 2001 Structure of the coding region and mRNA variants of the apyrase gene from pea (Pisum sativum) Acta Physiol Plant 23 3 13
    • (2001) Acta Physiol Plant , vol.23 , pp. 3-13
    • Shibata, K.1    Abe, S.2    Davies, E.3
  • 38
    • 0033428162 scopus 로고    scopus 로고
    • Apyrase from pea stems: Isolation, purification, characterization and identification of a NTPase from the cytoskeleton fraction of pea stem tissue
    • K Shibata Y Morita S Abe B Stankovic E Davies 1999 Apyrase from pea stems: Isolation, purification, characterization and identification of a NTPase from the cytoskeleton fraction of pea stem tissue Plant Physiol Biochem 37 881 888
    • (1999) Plant Physiol Biochem , vol.37 , pp. 881-888
    • Shibata, K.1    Morita, Y.2    Abe, S.3    Stankovic, B.4    Davies, E.5
  • 39
    • 0029807346 scopus 로고    scopus 로고
    • Localization and binding characteristics of a high-affinity binding site for N-acetylchitooligosaccharide elicitor in the plasma membrane from suspension cultured rice cells suggest a role as a receptor for the elicitor signal at the cell surface
    • N Shibuya N Ebisu Y Kamada H Kaku J Cohn Y Ito 1996 Localization and binding characteristics of a high-affinity binding site for N- acetylchitooligosaccharide elicitor in the plasma membrane from suspension cultured rice cells suggest a role as a receptor for the elicitor signal at the cell surface Plant Cell Physiol 37 894 898
    • (1996) Plant Cell Physiol , vol.37 , pp. 894-898
    • Shibuya, N.1    Ebisu, N.2    Kamada, Y.3    Kaku, H.4    Cohn, J.5    Ito, Y.6
  • 42
    • 0030932773 scopus 로고    scopus 로고
    • The role of suppressors in determining host-parasite specificities in plant cells
    • T Shiraishi T Yamada Y Ichinose A Kiba K Toyoda 1997 The role of suppressors in determining host-parasite specificities in plant cells Int Rev Cytol 172 55 93
    • (1997) Int Rev Cytol , vol.172 , pp. 55-93
    • Shiraishi, T.1    Yamada, T.2    Ichinose, Y.3    Kiba, A.4    Toyoda, K.5
  • 44
    • 0032575263 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of a human brain ecto-apyrase related to both the ecto-ATPase and CD39 ecto-apyrase
    • TM Smith TL Kirley 1998 Cloning, sequencing and expression of a human brain ecto-apyrase related to both the ecto-ATPase and CD39 ecto-apyrase Biochem Biophys Acta 1386 68 78
    • (1998) Biochem Biophys Acta , vol.1386 , pp. 68-78
    • Smith, T.M.1    Kirley, T.L.2
  • 45
    • 0028401517 scopus 로고
    • Synthesis of a glycopeptide with phytoalexin elicitor activity I. Synthesis of a triglycosyl L-serine and triglycosyl L-serine-L-proline dipeptide
    • T Takeda T Kanemitsu M Ishiguro Y Ogihara M Matsubara 1994 Synthesis of a glycopeptide with phytoalexin elicitor activity I. Synthesis of a triglycosyl L-serine and triglycosyl L-serine-L-proline dipeptide Carbohydr Res 256 59 69
    • (1994) Carbohydr Res , vol.256 , pp. 59-69
    • Takeda, T.1    Kanemitsu, T.2    Ishiguro, M.3    Ogihara, Y.4    Matsubara, M.5
  • 46
    • 0033080493 scopus 로고    scopus 로고
    • Apyrase functions in plant phosphate nutrition and mobilized phosphate from extracellular ATP
    • C Thomas Y Sun K Naus A Lioyd S Roux 1999 Apyrase functions in plant phosphate nutrition and mobilized phosphate from extracellular ATP Plant Physiol 119 543 551
    • (1999) Plant Physiol , vol.119 , pp. 543-551
    • Thomas, C.1    Sun, Y.2    Naus, K.3    Lioyd, A.4    Roux, S.5
  • 49
    • 0029025791 scopus 로고
    • A supprescin from a phytopathogenic fungus deactivates transcription of a plant defense gene encoding phenylalanine ammonia-lyase
    • M Wada H Kato K Malik P Sriprasertsak Y Ichinose T Shiraishi T Yamada 1995 A supprescin from a phytopathogenic fungus deactivates transcription of a plant defense gene encoding phenylalanine ammonia-lyase J Mol Biol 249 513 519
    • (1995) J Mol Biol , vol.249 , pp. 513-519
    • Wada, M.1    Kato, H.2    Malik, K.3    Sriprasertsak, P.4    Ichinose, Y.5    Shiraishi, T.6    Yamada, T.7
  • 50
    • 0037382949 scopus 로고    scopus 로고
    • Multiherbicide tolerance conferred by AtPgp1 and apyrase overexpression in Arabidopsis thaliana
    • B Windsor SJ Roux A Lloyd 2003 Multiherbicide tolerance conferred by AtPgp1 and apyrase overexpression in Arabidopsis thaliana Nat Biotechnol 21 428 433
    • (2003) Nat Biotechnol , vol.21 , pp. 428-433
    • Windsor, B.1    Roux, S.J.2    Lloyd, A.3
  • 51
    • 0000332512 scopus 로고
    • Suppression of pisatin, phenylalanine ammonia-lyase mRNA, and chalcone synthase mRNA by putative pathogenicity factor from the fungus Mycosphaerella pinodes
    • T Yamada H Hashimoto T Shiraishi H Oku 1989 Suppression of pisatin, phenylalanine ammonia-lyase mRNA, and chalcone synthase mRNA by putative pathogenicity factor from the fungus Mycosphaerella pinodes Mol Plant Microbe Interact 2 256 261
    • (1989) Mol Plant Microbe Interact , vol.2 , pp. 256-261
    • Yamada, T.1    Hashimoto, H.2    Shiraishi, T.3    Oku, H.4
  • 52
    • 0027134948 scopus 로고
    • A specific binding site on soybean membranes for a phytoalexin elicitor released from fungal cell walls by β-1,3-endoglucanase
    • M Yoshikawa K Sugimoto 1993 A specific binding site on soybean membranes for a phytoalexin elicitor released from fungal cell walls by β-1,3-endoglucanase Plant Cell Physiol 34 1229 1237
    • (1993) Plant Cell Physiol , vol.34 , pp. 1229-1237
    • Yoshikawa, M.1    Sugimoto, K.2
  • 53
    • 0000721809 scopus 로고
    • Suppression of pisatin production and ATPase activity in pea plasma membranes by orthovanadate, verapamil and a suppressor from Mycosphaerella pinodes
    • H Yoshioka T Shiraishi T Yamada Y Ichinose H Oku 1990 Suppression of pisatin production and ATPase activity in pea plasma membranes by orthovanadate, verapamil and a suppressor from Mycosphaerella pinodes Plant Cell Physiol 31 1139 1146
    • (1990) Plant Cell Physiol , vol.31 , pp. 1139-1146
    • Yoshioka, H.1    Shiraishi, T.2    Yamada, T.3    Ichinose, Y.4    Oku, H.5
  • 54
    • 0000692315 scopus 로고
    • Orthovanadate suppresses accumulation of phenylalanine ammonia-lyase mRNA and chalcone synthase mRNA in pea epicotyls induced by elicitor from Mycosphaerella pinodes
    • H Yoshioka T Shiraishi S Kawamata K Nasu T Yamada Y Ichinose H Oku 1992a Orthovanadate suppresses accumulation of phenylalanine ammonia-lyase mRNA and chalcone synthase mRNA in pea epicotyls induced by elicitor from Mycosphaerella pinodes Plant Cell Physiol 33 201 204
    • (1992) Plant Cell Physiol , vol.33 , pp. 201-204
    • Yoshioka, H.1    Shiraishi, T.2    Kawamata, S.3    Nasu, K.4    Yamada, T.5    Ichinose, Y.6    Oku, H.7
  • 55
    • 0009668391 scopus 로고
    • Suppression of activation of chitinase and β-1,3-glucanase in pea epicotyls by orthovanadate and suppressor from Mycosphaerella pinodes
    • H Yoshioka T Shiraishi K Nasu T Yamada Y Ichinose H Oku 1992b Suppression of activation of chitinase and β-1,3-glucanase in pea epicotyls by orthovanadate and suppressor from Mycosphaerella pinodes Ann Phytopathol Soc Jpn 58 405 410
    • (1992) Ann Phytopathol Soc Jpn , vol.58 , pp. 405-410
    • Yoshioka, H.1    Shiraishi, T.2    Nasu, K.3    Yamada, T.4    Ichinose, Y.5    Oku, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.