메뉴 건너뛰기




Volumn 47, Issue 1, 2010, Pages 53-65

The Botrytis cinerea aspartic proteinase family

Author keywords

Bioinformatics; Evolution; Gray mould; Phylogeny; Plant pathogen; Proteinase

Indexed keywords

ASPARTIC PROTEINASE; FUNGAL PROTEIN;

EID: 71249099770     PISSN: 10871845     EISSN: 10960937     Source Type: Journal    
DOI: 10.1016/j.fgb.2009.10.008     Document Type: Article
Times cited : (86)

References (61)
  • 1
    • 0025276666 scopus 로고
    • Revised 2.3 a structure of porcine pepsin: evidence for a flexible subdomain
    • Abad-Zapatero C., Rydel T.J., and Erickson J. Revised 2.3 a structure of porcine pepsin: evidence for a flexible subdomain. Proteins 8 (1990) 62-81
    • (1990) Proteins , vol.8 , pp. 62-81
    • Abad-Zapatero, C.1    Rydel, T.J.2    Erickson, J.3
  • 2
    • 68949128584 scopus 로고    scopus 로고
    • Homothallic and heterothallic mating in the opportunistic pathogen Candida albicans
    • Alby K., Schaefer D., and Bennett R.J. Homothallic and heterothallic mating in the opportunistic pathogen Candida albicans. Nature 460 (2009) 890-894
    • (2009) Nature , vol.460 , pp. 890-894
    • Alby, K.1    Schaefer, D.2    Bennett, R.J.3
  • 7
    • 29444452190 scopus 로고    scopus 로고
    • The endo-β-1, 4-xylanase Xyn11A is required for virulence in Botrytis cinerea
    • Brito N., Espino J.J., and Gonzalez C. The endo-β-1, 4-xylanase Xyn11A is required for virulence in Botrytis cinerea. Mol. Plant-Microbe Interact. 19 (2006) 25-32
    • (2006) Mol. Plant-Microbe Interact. , vol.19 , pp. 25-32
    • Brito, N.1    Espino, J.J.2    Gonzalez, C.3
  • 9
    • 71249126900 scopus 로고    scopus 로고
    • Yapsin1
    • Barrett A.J., Rawlings N.D., and Woessner J.F. (Eds), Elsevier Academic Press, Amsterdam
    • Cawley N.X., and Loh Y.P. Yapsin1. In: Barrett A.J., Rawlings N.D., and Woessner J.F. (Eds). Handbook of Proteolytic Enzymes (2004), Elsevier Academic Press, Amsterdam 128-131
    • (2004) Handbook of Proteolytic Enzymes , pp. 128-131
    • Cawley, N.X.1    Loh, Y.P.2
  • 10
    • 0842313260 scopus 로고    scopus 로고
    • Prediction of proprotein convertase cleavage sites
    • Duckert P., Brunak S., and Blom N. Prediction of proprotein convertase cleavage sites. Protein Eng. Des. Sel. 17 (2004) 107-112
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 107-112
    • Duckert, P.1    Brunak, S.2    Blom, N.3
  • 11
    • 0036882390 scopus 로고    scopus 로고
    • Structure and mechanism of the pepsin-like family of aspartic peptidases
    • Dunn B.M. Structure and mechanism of the pepsin-like family of aspartic peptidases. Chem. Rev. 102 (2002) 4431-4458
    • (2002) Chem. Rev. , vol.102 , pp. 4431-4458
    • Dunn, B.M.1
  • 12
    • 1442348239 scopus 로고    scopus 로고
    • A sensitive predictor for potential GPI lipid modification sites in fungal protein sequences and its application to genome-wide studies for Aspergillus nidulans, Candida albicans, Neurospora crassa, Saccharomyces cerevisiae, and Schizosaccharomyces pombe
    • Eisenhaber B., Schneider G., Wildpaner M., and Eisenhaber F. A sensitive predictor for potential GPI lipid modification sites in fungal protein sequences and its application to genome-wide studies for Aspergillus nidulans, Candida albicans, Neurospora crassa, Saccharomyces cerevisiae, and Schizosaccharomyces pombe. J. Mol. Biol. 337 (2004) 243-253
    • (2004) J. Mol. Biol. , vol.337 , pp. 243-253
    • Eisenhaber, B.1    Schneider, G.2    Wildpaner, M.3    Eisenhaber, F.4
  • 13
    • 28944444705 scopus 로고    scopus 로고
    • Botrytis cinerea endo-β-1, 4-glucanase Cel5A is expressed during infection but is not required for pathogenesis
    • Espino J.J., Brito N., Noda J., and Gonzalez C. Botrytis cinerea endo-β-1, 4-glucanase Cel5A is expressed during infection but is not required for pathogenesis. Physiol. Mol. Plant Pathol. 66 (2005) 213-221
    • (2005) Physiol. Mol. Plant Pathol. , vol.66 , pp. 213-221
    • Espino, J.J.1    Brito, N.2    Noda, J.3    Gonzalez, C.4
  • 14
    • 0000122573 scopus 로고
    • PHYLIP - phylogeny inference package (version 3.2)
    • Felsenstein J. PHYLIP - phylogeny inference package (version 3.2). Cladistics 5 (1989) 164-166
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 16
    • 4143051701 scopus 로고    scopus 로고
    • Crystal structure of aspartic proteinase from Irpex lacteus in complex with inhibitor pepstatin
    • Fujimoto Z., Fujii Y., Kaneko S., Kobayashi H., and Mizuno H. Crystal structure of aspartic proteinase from Irpex lacteus in complex with inhibitor pepstatin. J. Mol. Biol. 341 (2004) 1227-1235
    • (2004) J. Mol. Biol. , vol.341 , pp. 1227-1235
    • Fujimoto, Z.1    Fujii, Y.2    Kaneko, S.3    Kobayashi, H.4    Mizuno, H.5
  • 17
    • 33749991922 scopus 로고    scopus 로고
    • Fungal yapsins and cell wall: a unique family of aspartic peptidases for a distinctive cellular function
    • Gagnon-Arsenault I., Tremblay J., and Bourbonnais Y. Fungal yapsins and cell wall: a unique family of aspartic peptidases for a distinctive cellular function. FEMS Yeast Res. 6 (2006) 966-978
    • (2006) FEMS Yeast Res. , vol.6 , pp. 966-978
    • Gagnon-Arsenault, I.1    Tremblay, J.2    Bourbonnais, Y.3
  • 18
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by Maximum Likelihood
    • Guindon S., and Gascuel O. A simple, fast, and accurate algorithm to estimate large phylogenies by Maximum Likelihood. Syst. Biol. 52 (2003) 696-704
    • (2003) Syst. Biol. , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 19
    • 0036016444 scopus 로고    scopus 로고
    • The cell wall hydroxyproline-rich glycoprotein RSH is essential for normal embryo development in Arabidopsis
    • Hall Q., and Cannon M.C. The cell wall hydroxyproline-rich glycoprotein RSH is essential for normal embryo development in Arabidopsis. Plant Cell 14 (2002) 1161-1172
    • (2002) Plant Cell , vol.14 , pp. 1161-1172
    • Hall, Q.1    Cannon, M.C.2
  • 20
    • 0002364972 scopus 로고
    • Yeasts-metabolism of nitrogen compounds
    • Fleet G.H. (Ed), Harwood Academic, Chur, Switzerland
    • Henschke P.A., and Jiranek V. Yeasts-metabolism of nitrogen compounds. In: Fleet G.H. (Ed). Wine microbiology and biotechnology (1993), Harwood Academic, Chur, Switzerland 77-164
    • (1993) Wine microbiology and biotechnology , pp. 77-164
    • Henschke, P.A.1    Jiranek, V.2
  • 23
    • 71249109523 scopus 로고    scopus 로고
    • Jarvis, W. R. 1977. Botryotinia and Botrytis species: taxonomy, physiology, and pathogenicity. Monogr. Res. Branch Can. Dept. Agric. 15.
    • Jarvis, W. R. 1977. Botryotinia and Botrytis species: taxonomy, physiology, and pathogenicity. Monogr. Res. Branch Can. Dept. Agric. 15.
  • 24
    • 0034254266 scopus 로고    scopus 로고
    • Direct interaction of resistance gene and avirulence gene products confers rice Blast resistance
    • Jia Y., McAdams S.A., Bryan G.T., Hershey H.P., and Valent B. Direct interaction of resistance gene and avirulence gene products confers rice Blast resistance. EMBO J. 19 (2000) 4004-4014
    • (2000) EMBO J. , vol.19 , pp. 4004-4014
    • Jia, Y.1    McAdams, S.A.2    Bryan, G.T.3    Hershey, H.P.4    Valent, B.5
  • 25
    • 22544465583 scopus 로고    scopus 로고
    • Necrotising activity of five Botrytis cinerea endopolygalacturonases produced in Pichia pastoris
    • Kars I., Krooshof G., Wagemakers C.A.M., Joosten R., Benen J.A.E., and van Kan J.A.L. Necrotising activity of five Botrytis cinerea endopolygalacturonases produced in Pichia pastoris. Plant J. 43 (2005) 213-225
    • (2005) Plant J. , vol.43 , pp. 213-225
    • Kars, I.1    Krooshof, G.2    Wagemakers, C.A.M.3    Joosten, R.4    Benen, J.A.E.5    van Kan, J.A.L.6
  • 26
    • 33646342452 scopus 로고    scopus 로고
    • Functional analysis of Botrytis cinerea pectin methylesterase genes by PCR-based targeted mutagenesis: Bcpme1 and Bcpme2 are dispensable for virulence of strain B05.10
    • Kars I., Wagemakers C.A.M., McCalman M., and van Kan J.A.L. Functional analysis of Botrytis cinerea pectin methylesterase genes by PCR-based targeted mutagenesis: Bcpme1 and Bcpme2 are dispensable for virulence of strain B05.10. Mol. Plant Pathol. 6 (2005) 641-652
    • (2005) Mol. Plant Pathol. , vol.6 , pp. 641-652
    • Kars, I.1    Wagemakers, C.A.M.2    McCalman, M.3    van Kan, J.A.L.4
  • 27
    • 0031956497 scopus 로고    scopus 로고
    • Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes
    • Khan A.R., and James M.N. Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes. Protein Sci. 7 (1998) 815-836
    • (1998) Protein Sci. , vol.7 , pp. 815-836
    • Khan, A.R.1    James, M.N.2
  • 28
    • 0029041261 scopus 로고
    • Processing enzymes of the pepsin family: yeast aspartic proteinase3 and pro-opiomelanocortin converting enzyme
    • Loh Y.P., and Cawley N.X. Processing enzymes of the pepsin family: yeast aspartic proteinase3 and pro-opiomelanocortin converting enzyme. Methods Enzymol. 248 (1995) 136-146
    • (1995) Methods Enzymol. , vol.248 , pp. 136-146
    • Loh, Y.P.1    Cawley, N.X.2
  • 32
    • 0001709810 scopus 로고
    • The roles of aspartic proteinase and endo-pectin lyase enzymes in the primary stages of infection and pathogenesis of various host tissues by different isolates of Botrytis cinerea Pers ex
    • Movahedi S., and Heale J.B. The roles of aspartic proteinase and endo-pectin lyase enzymes in the primary stages of infection and pathogenesis of various host tissues by different isolates of Botrytis cinerea Pers ex. Pers. Physiol. Mol. Plant Pathol. 36 (1990) 303-324
    • (1990) Pers. Physiol. Mol. Plant Pathol. , vol.36 , pp. 303-324
    • Movahedi, S.1    Heale, J.B.2
  • 33
    • 0030136788 scopus 로고    scopus 로고
    • Three extracellular proteases from Cochliobolus carbonum: cloning and targeted disruption of ALP1
    • Murphy J.M., and Walton J.D. Three extracellular proteases from Cochliobolus carbonum: cloning and targeted disruption of ALP1. Mol. Plant-Microbe Interact. 9 (1996) 290-297
    • (1996) Mol. Plant-Microbe Interact. , vol.9 , pp. 290-297
    • Murphy, J.M.1    Walton, J.D.2
  • 34
    • 0022262821 scopus 로고
    • Clear background and highly sensitive protein staining with Coomassie blue dyes in polyacrylamide gels: a systematic analysis
    • Neuhoff V., Stamm R., and Eibl H. Clear background and highly sensitive protein staining with Coomassie blue dyes in polyacrylamide gels: a systematic analysis. Electrophoresis 6 (1985) 427-448
    • (1985) Electrophoresis , vol.6 , pp. 427-448
    • Neuhoff, V.1    Stamm, R.2    Eibl, H.3
  • 36
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., and von Heijne G. 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
  • 37
    • 35248843062 scopus 로고    scopus 로고
    • Methodological improvements in the expression of foreign genes and in gene replacement in the phytopathogenic fungus Botrytis cinerea
    • Noda J., Brito N., Espino J.J., and Gonzalez C. Methodological improvements in the expression of foreign genes and in gene replacement in the phytopathogenic fungus Botrytis cinerea. Mol. Plant Pathol. 8 (2007) 811-816
    • (2007) Mol. Plant Pathol. , vol.8 , pp. 811-816
    • Noda, J.1    Brito, N.2    Espino, J.J.3    Gonzalez, C.4
  • 38
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: a novel method for multiple sequence alignments
    • Notredame C., Higgins D.G., and Heringa J. T-Coffee: a novel method for multiple sequence alignments. J. Mol. Biol. 302 (2000) 205-217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 39
    • 34347392289 scopus 로고    scopus 로고
    • The structure and function of Saccharomyces cerevisiae proteinase A
    • Parr C.L., Keates R.A., Bryksa B.C., Ogawa M., and Yada R.Y. The structure and function of Saccharomyces cerevisiae proteinase A. Yeast 24 (2007) 467-480
    • (2007) Yeast , vol.24 , pp. 467-480
    • Parr, C.L.1    Keates, R.A.2    Bryksa, B.C.3    Ogawa, M.4    Yada, R.Y.5
  • 41
    • 38749105868 scopus 로고    scopus 로고
    • The MEROPS batch BLAST: a tool to detect peptidases and their non-peptidase homologues in a genome
    • Rawlings N.D., and Morton F.R. The MEROPS batch BLAST: a tool to detect peptidases and their non-peptidase homologues in a genome. Biochimie 90 (2008) 243-259
    • (2008) Biochimie , vol.90 , pp. 243-259
    • Rawlings, N.D.1    Morton, F.R.2
  • 42
    • 46249098663 scopus 로고    scopus 로고
    • Sulphur and nitrogen regulation of the protease-encoding ACP1 gene in the fungus Botrytis cinerea: correlation with a phospholipase D activity
    • Rolland S.G., and Bruel C.A. Sulphur and nitrogen regulation of the protease-encoding ACP1 gene in the fungus Botrytis cinerea: correlation with a phospholipase D activity. Microbiology 154 (2008) 1464-1473
    • (2008) Microbiology , vol.154 , pp. 1464-1473
    • Rolland, S.G.1    Bruel, C.A.2
  • 43
    • 0035181818 scopus 로고    scopus 로고
    • The role of G protein alpha subunits in the infection process of the gray mold fungus Botrytis cinerea
    • Schulze Gronover C., Kasulke D., Tudzynski P., and Tudzynski B. The role of G protein alpha subunits in the infection process of the gray mold fungus Botrytis cinerea. Mol. Plant-Microbe Interact. 14 (2001) 1293-1302
    • (2001) Mol. Plant-Microbe Interact. , vol.14 , pp. 1293-1302
    • Schulze Gronover, C.1    Kasulke, D.2    Tudzynski, P.3    Tudzynski, B.4
  • 45
    • 33746659356 scopus 로고    scopus 로고
    • Generation and analysis of expressed sequence tags from Botrytis cinerea
    • Silva E., Valdés J., Holmes D., Shmaryahu A., and Valenzuela P.D.T. Generation and analysis of expressed sequence tags from Botrytis cinerea. Biol. Res. 39 (2006) 367-376
    • (2006) Biol. Res. , vol.39 , pp. 367-376
    • Silva, E.1    Valdés, J.2    Holmes, D.3    Shmaryahu, A.4    Valenzuela, P.D.T.5
  • 46
    • 27644495321 scopus 로고    scopus 로고
    • Proteomic analysis of secreted proteins from Trichoderma harzianum: identification of a fungal cell wall-induced aspartic protease
    • Suárez M.B., Sanz L., Chamorro M.I., Rey M., González F.J., Llobell A., and Monte E. Proteomic analysis of secreted proteins from Trichoderma harzianum: identification of a fungal cell wall-induced aspartic protease. Fungal Genet. Biol. 42 (2005) 924-934
    • (2005) Fungal Genet. Biol. , vol.42 , pp. 924-934
    • Suárez, M.B.1    Sanz, L.2    Chamorro, M.I.3    Rey, M.4    González, F.J.5    Llobell, A.6    Monte, E.7
  • 47
    • 34247248872 scopus 로고    scopus 로고
    • Characterization of genes encoding novel peptidasesin the biocontrol fungus Trichoderma harzianum CECT 2413 using the TrichoEST functional genomics approach
    • Suárez M.B., Vizcaíno J.A., Llobell A., and Monte E. Characterization of genes encoding novel peptidasesin the biocontrol fungus Trichoderma harzianum CECT 2413 using the TrichoEST functional genomics approach. Curr. Genet. 51 (2007) 331-342
    • (2007) Curr. Genet. , vol.51 , pp. 331-342
    • Suárez, M.B.1    Vizcaíno, J.A.2    Llobell, A.3    Monte, E.4
  • 48
    • 0032190199 scopus 로고    scopus 로고
    • The endopolygalacturonase gene Bcpg1 is required for full virulence of Botrytis cinerea
    • ten Have A., Mulder W., Visser J., and van Kan J.A.L. The endopolygalacturonase gene Bcpg1 is required for full virulence of Botrytis cinerea. Mol. Plant-Microbe Interact. 11 (1998) 1009-1016
    • (1998) Mol. Plant-Microbe Interact. , vol.11 , pp. 1009-1016
    • ten Have, A.1    Mulder, W.2    Visser, J.3    van Kan, J.A.L.4
  • 49
    • 0010052062 scopus 로고    scopus 로고
    • The contribution of cell wall degrading enzymes to pathogenesis of fungal plant pathogens (review)
    • Kempken F. (Ed), Springer-Verlag, Berlin, Heidelberg (Chapter 17)
    • ten Have A., Tenberge K., Benen J.A.E., Tudzynski P., Visser J., and van Kan J.A.L. The contribution of cell wall degrading enzymes to pathogenesis of fungal plant pathogens (review). In: Kempken F. (Ed). The Mycota XI Agricultural Applications vol. 20 (2002), Springer-Verlag, Berlin, Heidelberg 341-358 (Chapter 17)
    • (2002) The Mycota XI Agricultural Applications , vol.20 , pp. 341-358
    • ten Have, A.1    Tenberge, K.2    Benen, J.A.E.3    Tudzynski, P.4    Visser, J.5    van Kan, J.A.L.6
  • 50
    • 4344605203 scopus 로고    scopus 로고
    • An aspartic proteinase gene family in the filamentous fungus Botrytis cinerea contains members with novel features
    • ten Have A., Dekkers E., Kay J., Phylip L.H., and van Kan J.A.L. An aspartic proteinase gene family in the filamentous fungus Botrytis cinerea contains members with novel features. Microbiology 150 (2004) 2475-2489
    • (2004) Microbiology , vol.150 , pp. 2475-2489
    • ten Have, A.1    Dekkers, E.2    Kay, J.3    Phylip, L.H.4    van Kan, J.A.L.5
  • 52
    • 33646359197 scopus 로고    scopus 로고
    • Licensed to kill: the lifestyle of a necrotrophic plant pathogen
    • van Kan J.A.L. Licensed to kill: the lifestyle of a necrotrophic plant pathogen. Trends Plant Sci. 11 (2006) 247-253
    • (2006) Trends Plant Sci. , vol.11 , pp. 247-253
    • van Kan, J.A.L.1
  • 54
    • 33748941620 scopus 로고    scopus 로고
    • Significance of inducible defense-related proteins in infected plants
    • van Loon L.C., Rep M., and Pieterse C.M. Significance of inducible defense-related proteins in infected plants. Ann. Rev. Phytopathol. 44 (2006) 135-162
    • (2006) Ann. Rev. Phytopathol. , vol.44 , pp. 135-162
    • van Loon, L.C.1    Rep, M.2    Pieterse, C.M.3
  • 55
  • 57
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel D., and Flügge U.I. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138 (1984) 141-143
    • (1984) Anal. Biochem. , vol.138 , pp. 141-143
    • Wessel, D.1    Flügge, U.I.2
  • 59
    • 84944045394 scopus 로고    scopus 로고
    • Saccharopepsin
    • Barrett A.J., Rawlings N.D., and Woessner J.F. (Eds), Elsevier Academic Press, Amsterdam
    • Winther J.R., Phylip L.H., and Kay J. Saccharopepsin. In: Barrett A.J., Rawlings N.D., and Woessner J.F. (Eds). Handbook of Proteolytic Enzymes (2004), Elsevier Academic Press, Amsterdam 87-90
    • (2004) Handbook of Proteolytic Enzymes , pp. 87-90
    • Winther, J.R.1    Phylip, L.H.2    Kay, J.3
  • 60
    • 0023873352 scopus 로고
    • Functional characterization of Asp-317 mutant of human renin expressed in COS cells
    • Yamauchi T., Nagahama M., Hori H., and Murakami K. Functional characterization of Asp-317 mutant of human renin expressed in COS cells. FEBS Lett. 230 (1988) 205-208
    • (1988) FEBS Lett. , vol.230 , pp. 205-208
    • Yamauchi, T.1    Nagahama, M.2    Hori, H.3    Murakami, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.