메뉴 건너뛰기




Volumn 339, Issue 1, 2004, Pages 173-183

Structural analysis of the human Golgi-associated plant pathogenesis related protein GAPR-1 implicates dimerization as a regulatory mechanism

Author keywords

MALDI TOF, matrix assisted laser desorption time of flight mass spectroscopy; plant pathogenesis related protein; PR, pathogenesis related; PR 1; quasi elastic light scattering; X ray crystallography; yeast two hybrid screening

Indexed keywords

AMINO ACID; GOLGI ASSOCIATED PLANT PATHOGENESIS RELATED PROTEIN 1; PROTEIN; SERINE PROTEINASE; UNCLASSIFIED DRUG;

EID: 2342453841     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.03.015     Document Type: Article
Times cited : (64)

References (51)
  • 1
    • 0014941283 scopus 로고
    • Hypersensitivity to viruses, temperature and soluble proteins in Nicotiana xanthi n.c. Appearance of new macromolecules at the repression of viral synthesis
    • Gianinazzi S., Martin C., Vallee J.C. Hypersensitivity to viruses, temperature and soluble proteins in Nicotiana xanthi n.c. Appearance of new macromolecules at the repression of viral synthesis. C. R. Acad. Sci. Hebd. Seances Acad. Sci. D. 270:1970;2383-2386
    • (1970) C. R. Acad. Sci. Hebd. Seances Acad. Sci. D , vol.270 , pp. 2383-2386
    • Gianinazzi, S.1    Martin, C.2    Vallee, J.C.3
  • 2
    • 0014736229 scopus 로고
    • Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. "samsun" and "samsun NN". II. Changes in protein constitution after infection with tobacco mosaic virus
    • van Loon L.C., van Kammen A. Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. "Samsun" and "Samsun NN". II. Changes in protein constitution after infection with tobacco mosaic virus. Virology. 40:1970;190-211
    • (1970) Virology , vol.40 , pp. 190-211
    • Van Loon, L.C.1    Van Kammen, A.2
  • 4
    • 0030481542 scopus 로고    scopus 로고
    • Death don't have no mercy: Cell death programs in plant microbe interactions
    • Dangl J.L., Dietrich R.A., Richberg M.H. Death don't have no mercy: cell death programs in plant microbe interactions. Plant Cell. 8:1996;1793-1807
    • (1996) Plant Cell , vol.8 , pp. 1793-1807
    • Dangl, J.L.1    Dietrich, R.A.2    Richberg, M.H.3
  • 6
    • 0001376743 scopus 로고
    • Pathogenesis-related proteins
    • van Loon L.C. Pathogenesis-related proteins. Plant Mol. Biol. 4:1985;111-116
    • (1985) Plant Mol. Biol. , vol.4 , pp. 111-116
    • Van Loon, L.C.1
  • 8
    • 33644535944 scopus 로고
    • Pathogenesis related proteins of plants
    • Linthorst H.J.M. Pathogenesis related proteins of plants. Crit. Rev. Plant Sci. 10:1991;123-150
    • (1991) Crit. Rev. Plant Sci. , vol.10 , pp. 123-150
    • Linthorst, H.J.M.1
  • 9
    • 0033179482 scopus 로고    scopus 로고
    • The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins
    • Van Loon L.C., Van Strien E.A. The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins. Physiol. Mol. Plant Pathol. 55:1999;85-97
    • (1999) Physiol. Mol. Plant Pathol. , vol.55 , pp. 85-97
    • Van Loon, L.C.1    Van Strien, E.A.2
  • 10
    • 0032974640 scopus 로고    scopus 로고
    • Plant pathogenesis-related proteins: Molecular mechanisms of gene expression and protein function
    • Kitajima S., Sato F. Plant pathogenesis-related proteins: molecular mechanisms of gene expression and protein function. J. Biochem. (Tokyo). 125:1999;1-8
    • (1999) J. Biochem. (Tokyo) , vol.125 , pp. 1-8
    • Kitajima, S.1    Sato, F.2
  • 11
    • 0029294601 scopus 로고
    • Pathogenesis-related PR-1 proteins are antifungal. Isolation and characterization of three 14-kilodalton proteins of tomato and of a basic PR-1 of tobacco with inhibitory activity against Phytophthora infestans
    • Niderman T., Genetet I., Bruyere T., Gees R., Stintzi A., Legrand M., et al. Pathogenesis-related PR-1 proteins are antifungal. Isolation and characterization of three 14-kilodalton proteins of tomato and of a basic PR-1 of tobacco with inhibitory activity against Phytophthora infestans. Plant Physiol. 108:1995;17-27
    • (1995) Plant Physiol. , vol.108 , pp. 17-27
    • Niderman, T.1    Genetet, I.2    Bruyere, T.3    Gees, R.4    Stintzi, A.5    Legrand, M.6
  • 12
    • 0033033724 scopus 로고    scopus 로고
    • Interaction of NPR1 with basic leucine zipper protein transcription factors that bind sequences required for salicylic acid induction of the PR-1 gene
    • Zhang Y., Fan W., Kinkema M., Li X., Dong X. Interaction of NPR1 with basic leucine zipper protein transcription factors that bind sequences required for salicylic acid induction of the PR-1 gene. Proc. Natl Acad. Sci. USA. 96:1999;6523-6528
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6523-6528
    • Zhang, Y.1    Fan, W.2    Kinkema, M.3    Li, X.4    Dong, X.5
  • 14
    • 0033662422 scopus 로고    scopus 로고
    • The transcriptome of Arabidopsis thaliana during systemic acquired resistance
    • Maleck K., Levine A., Eulgem T., Morgan A., Schmid J., Lawton K.A., et al. The transcriptome of Arabidopsis thaliana during systemic acquired resistance. Nature Genet. 26:2000;403-410
    • (2000) Nature Genet , vol.26 , pp. 403-410
    • Maleck, K.1    Levine, A.2    Eulgem, T.3    Morgan, A.4    Schmid, J.5    Lawton, K.A.6
  • 15
    • 0036237996 scopus 로고    scopus 로고
    • Isolation and characterization of broad-spectrum disease-resistant Arabidopsis mutants
    • Maleck K., Neuenschwander U., Cade R.M., Dietrich R.A., Dangl J.L., Ryals J.A. Isolation and characterization of broad-spectrum disease-resistant Arabidopsis mutants. Genetics. 160:2002;1661-1671
    • (2002) Genetics , vol.160 , pp. 1661-1671
    • Maleck, K.1    Neuenschwander, U.2    Cade, R.M.3    Dietrich, R.A.4    Dangl, J.L.5    Ryals, J.A.6
  • 16
    • 0041731780 scopus 로고    scopus 로고
    • Isolation and characterization of a cone snail protease with homology to CRISP proteins of the pathogenesis-related protein superfamily
    • Milne T.J., Abbenante G., Tyndall J.D., Halliday J., Lewis R.J. Isolation and characterization of a cone snail protease with homology to CRISP proteins of the pathogenesis-related protein superfamily. J. Biol. Chem. 278:2003;31105-31110
    • (2003) J. Biol. Chem. , vol.278 , pp. 31105-31110
    • Milne, T.J.1    Abbenante, G.2    Tyndall, J.D.3    Halliday, J.4    Lewis, R.J.5
  • 17
    • 0027424323 scopus 로고
    • The Sc7/Sc14 gene family of Schizophyllum commune codes for extracellular proteins specifically expressed during fruit-body formation
    • Schuren F.H., Asgeirsdottir S.A., Kothe E.M., Scheer J.M., Wessels J.G. The Sc7/Sc14 gene family of Schizophyllum commune codes for extracellular proteins specifically expressed during fruit-body formation. J. Gen. Microbiol. 139:1993;2083-2090
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2083-2090
    • Schuren, F.H.1    Asgeirsdottir, S.A.2    Kothe, E.M.3    Scheer, J.M.4    Wessels, J.G.5
  • 18
    • 0027245545 scopus 로고
    • Sequence analysis and antigenic cross-reactivity of a venom allergen, antigen 5, from hornets, wasps, and yellow jackets
    • Lu G., Villalba M., Coscia M.R., Hoffman D.R., King T.P. Sequence analysis and antigenic cross-reactivity of a venom allergen, antigen 5, from hornets, wasps, and yellow jackets. J. Immunol. 150:1993;2823-2830
    • (1993) J. Immunol. , vol.150 , pp. 2823-2830
    • Lu, G.1    Villalba, M.2    Coscia, M.R.3    Hoffman, D.R.4    King, T.P.5
  • 19
    • 0030927284 scopus 로고    scopus 로고
    • A novel cDNA from Drosophila encoding a protein with similarity to mammalian cysteine-rich secretory proteins, wasp venom antigen 5, and plant group 1 pathogenesis-related proteins
    • Schreiber M.C., Karlo J.C., Kovalick G.E. A novel cDNA from Drosophila encoding a protein with similarity to mammalian cysteine-rich secretory proteins, wasp venom antigen 5, and plant group 1 pathogenesis-related proteins. Gene. 191:1997;135-141
    • (1997) Gene , vol.191 , pp. 135-141
    • Schreiber, M.C.1    Karlo, J.C.2    Kovalick, G.E.3
  • 20
    • 0030020880 scopus 로고    scopus 로고
    • SGP28, a novel matrix glycoprotein in specific granules of human neutrophils with similarity to a human testis-specific gene product and a rodent sperm-coating glycoprotein
    • Kjeldsen L., Cowland J.B., Johnsen A.H., Borregaard N. SGP28, a novel matrix glycoprotein in specific granules of human neutrophils with similarity to a human testis-specific gene product and a rodent sperm-coating glycoprotein. FEBS Letters. 380:1996;246-250
    • (1996) FEBS Letters , vol.380 , pp. 246-250
    • Kjeldsen, L.1    Cowland, J.B.2    Johnsen, A.H.3    Borregaard, N.4
  • 21
    • 0029925313 scopus 로고    scopus 로고
    • The human cysteine-rich secretory protein (CRISP) family. Primary structure and tissue distribution of CRISP-1, CRISP-2 and CRISP-3
    • Kratzschmar J., Haendler B., Eberspaecher U., Roosterman D., Donner P., Schleuning W.D. The human cysteine-rich secretory protein (CRISP) family. Primary structure and tissue distribution of CRISP-1, CRISP-2 and CRISP-3. Eur. J. Biochem. 236:1996;827-836
    • (1996) Eur. J. Biochem. , vol.236 , pp. 827-836
    • Kratzschmar, J.1    Haendler, B.2    Eberspaecher, U.3    Roosterman, D.4    Donner, P.5    Schleuning, W.D.6
  • 22
    • 0029057894 scopus 로고
    • The human glioma pathogenesis-related protein is structurally related to plant pathogenesis-related proteins and its gene is expressed specifically in brain tumors
    • Murphy E.V., Zhang Y., Zhu W., Biggs J. The human glioma pathogenesis-related protein is structurally related to plant pathogenesis-related proteins and its gene is expressed specifically in brain tumors. Gene. 159:1995;131-135
    • (1995) Gene , vol.159 , pp. 131-135
    • Murphy, E.V.1    Zhang, Y.2    Zhu, W.3    Biggs, J.4
  • 23
    • 0030597333 scopus 로고    scopus 로고
    • RTVP-1, a novel human gene with sequence similarity to genes of diverse species, is expressed in tumor cell lines of glial but not neuronal origin
    • Rich T., Chen P., Furman F., Huynh N., Israel M.A. RTVP-1, a novel human gene with sequence similarity to genes of diverse species, is expressed in tumor cell lines of glial but not neuronal origin. Gene. 180:1996;125-130
    • (1996) Gene , vol.180 , pp. 125-130
    • Rich, T.1    Chen, P.2    Furman, F.3    Huynh, N.4    Israel, M.A.5
  • 25
    • 0033582176 scopus 로고    scopus 로고
    • Pseudechetoxin: A peptide blocker of cyclic nucleotide-gated ion channels
    • Brown R.L., Haley T.L., West K.A., Crabb J.W. Pseudechetoxin: a peptide blocker of cyclic nucleotide-gated ion channels. Proc. Natl Acad. Sci. USA. 96:1999;754-759
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 754-759
    • Brown, R.L.1    Haley, T.L.2    West, K.A.3    Crabb, J.W.4
  • 27
    • 0037084502 scopus 로고    scopus 로고
    • Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex
    • Eberle H.B., Serrano R.L., Fullekrug J., Schlosser A., Lehmann W.D., Lottspeich F., et al. Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex. J. Cell Sci. 115:2002;827-838
    • (2002) J. Cell Sci. , vol.115 , pp. 827-838
    • Eberle, H.B.1    Serrano, R.L.2    Fullekrug, J.3    Schlosser, A.4    Lehmann, W.D.5    Lottspeich, F.6
  • 29
    • 0035576365 scopus 로고    scopus 로고
    • Major venom allergen of yellow jackets, Ves v 5: Structural characterization of a pathogenesis-related protein superfamily
    • Henriksen A., King T.P., Mirza O., Monsalve R.I., Meno K., Ipsen H., et al. Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily. Proteins: Struct. Funct. Genet. 45:2001;438-448
    • (2001) Proteins: Struct. Funct. Genet. , vol.45 , pp. 438-448
    • Henriksen, A.1    King, T.P.2    Mirza, O.3    Monsalve, R.I.4    Meno, K.5    Ipsen, H.6
  • 30
    • 0015935205 scopus 로고
    • The charge relay system in chymotrypsin and chymotrypsinogen
    • Fersht A.R., Sperling J. The charge relay system in chymotrypsin and chymotrypsinogen. J. Mol. Biol. 74:1973;137-149
    • (1973) J. Mol. Biol. , vol.74 , pp. 137-149
    • Fersht, A.R.1    Sperling, J.2
  • 31
  • 32
    • 1842614386 scopus 로고    scopus 로고
    • Crystal structure of a myristoylated CAP-23/NAP-22 N-terminal domain complexed with Ca(2+)/calmodulin
    • Matsubara M., Nakatsu T., Kato H., Taniguchi H. Crystal structure of a myristoylated CAP-23/NAP-22 N-terminal domain complexed with Ca(2+)/calmodulin. EMBO J. 23:2004;712-718
    • (2004) EMBO J. , vol.23 , pp. 712-718
    • Matsubara, M.1    Nakatsu, T.2    Kato, H.3    Taniguchi, H.4
  • 33
  • 37
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. D. 47:1991;110-119
    • (1991) Acta Crystallog. Sect. D , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 40
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito H., Fukuda Y., Murata K., Kimura A. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:1983;163-168
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 41
    • 0004270170 scopus 로고
    • F.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, & S. Kevin. New York: John Wiley & Sons
    • Ausubel F.M., Brent R., Kingston R.E., Moore D.D., Seidman J.G., Kevin S. Current Protocols in Molecular Biology. 1988;John Wiley & Sons, New York
    • (1988) Current Protocols in Molecular Biology
  • 42
    • 0026069437 scopus 로고
    • A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein β-adaptin
    • Serafini T., Stenbeck G., Brecht A., Lottspeich F., Orci L., Rothman J.E., Wieland F.T. A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein β-adaptin. Nature. 349:1991;215-220
    • (1991) Nature , vol.349 , pp. 215-220
    • Serafini, T.1    Stenbeck, G.2    Brecht, A.3    Lottspeich, F.4    Orci, L.5    Rothman, J.E.6    Wieland, F.T.7
  • 44
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. 15:1997;133-138
    • (1997) J. Mol. Graph. , vol.15 , pp. 133-138
    • Esnouf, R.M.1
  • 45
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merrit E.A.B., D J. Raster3D: photorealistic molecular graphics. Macromol. Crystallog. 277:1997;505-524
    • (1997) Macromol. Crystallog. , vol.277 , pp. 505-524
    • Merrit, E.A.B.1    D, J.2
  • 46
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucl. Acids Res. 25:1997;4876-4882
    • (1997) Nucl. Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 47
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton G.J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 48
    • 0032167924 scopus 로고    scopus 로고
    • Structure of a non-psychrophilic trypsin from a cold-adapted fish species
    • Schroder H.K., Willasen N.P., Smalas A.O. Structure of a non-psychrophilic trypsin from a cold-adapted fish species. Acta Crystallog. sect. D. 54:1998;780-798
    • (1998) Acta Crystallog. Sect. D , vol.54 , pp. 780-798
    • Schroder, H.K.1    Willasen, N.P.2    Smalas, A.O.3
  • 49
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 50
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B., Richards F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55:1971;379-400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 51
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computing Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.