메뉴 건너뛰기




Volumn 105, Issue 44, 2008, Pages 16876-16881

Crystal structure and activity of Bacillus subtilis YoaJ (EXLX1), a bacterial expansin that promotes root colonization

Author keywords

Family 45 endoglucanase; Lytic transglycosylase; Peptidoglycan; Plant cell wall; Plant microbe interactions

Indexed keywords

CELLULOSE; EXLX1 PROTEIN; GLYCOSIDASE; GLYCOSYLTRANSFERASE; PATULIN; PEPTIDOGLYCAN; POLYSACCHARIDE; UNCLASSIFIED DRUG;

EID: 55949096569     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0809382105     Document Type: Article
Times cited : (167)

References (38)
  • 2
    • 27644525170 scopus 로고    scopus 로고
    • Growth of the plant cell wall
    • Cosgrove DJ (2005) Growth of the plant cell wall. Nat Rev Mol Cell Biol 6:850-861.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 850-861
    • Cosgrove, D.J.1
  • 4
    • 0034699445 scopus 로고    scopus 로고
    • Loosening of plant cell walls by expansins
    • Cosgrove DJ (2000) Loosening of plant cell walls by expansins. Nature 407:321-326.
    • (2000) Nature , vol.407 , pp. 321-326
    • Cosgrove, D.J.1
  • 5
    • 33749536575 scopus 로고    scopus 로고
    • Crystal structure and activities of EXPB1 (Zea m 1), a β-expansin and group-1 pollen allergen from maize
    • Yennawar NH, Li LC, Dudzinski DM, Tabuchi A, Cosgrove DJ (2006) Crystal structure and activities of EXPB1 (Zea m 1), a β-expansin and group-1 pollen allergen from maize. Proc Natl Acad Sci USA 103:14664-14671.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 14664-14671
    • Yennawar, N.H.1    Li, L.C.2    Dudzinski, D.M.3    Tabuchi, A.4    Cosgrove, D.J.5
  • 6
    • 0027351945 scopus 로고
    • Structural models of primary cell walls in flowering plants: Consistency of molecular structure with the physical properties of the walls during growth
    • Carpita NC, Gibeaut DM (1993) Structural models of primary cell walls in flowering plants: Consistency of molecular structure with the physical properties of the walls during growth. Plant J 3:1-30.
    • (1993) Plant J , vol.3 , pp. 1-30
    • Carpita, N.C.1    Gibeaut, D.M.2
  • 7
    • 0036006037 scopus 로고    scopus 로고
    • Plant expansins are a complex multigene family with an ancient evolutionary origin
    • Li Y, et al. (2002) Plant expansins are a complex multigene family with an ancient evolutionary origin. Plant Physiol 128:854-864.
    • (2002) Plant Physiol , vol.128 , pp. 854-864
    • Li, Y.1
  • 8
    • 0842328851 scopus 로고    scopus 로고
    • Biocontrol of Bacillus subtilis against infection of Arabidopsis roots by Pseudomonas syringae is facilitated by biofilm formation and surfactin production
    • Bais HP, Fall R, Vivanco JM (2004) Biocontrol of Bacillus subtilis against infection of Arabidopsis roots by Pseudomonas syringae is facilitated by biofilm formation and surfactin production. Plant Physiol 134:307-319.
    • (2004) Plant Physiol , vol.134 , pp. 307-319
    • Bais, H.P.1    Fall, R.2    Vivanco, J.M.3
  • 9
    • 12444251680 scopus 로고    scopus 로고
    • Nomenclature for members of the expansin superfamily of genes and proteins
    • Kende H, et al. (2004) Nomenclature for members of the expansin superfamily of genes and proteins. Plant Mol Biol 55:311-314.
    • (2004) Plant Mol Biol , vol.55 , pp. 311-314
    • Kende, H.1
  • 10
    • 0033080967 scopus 로고    scopus 로고
    • A six-stranded double-psi β-barrel is shared by several protein superfamilies
    • Castillo RM, et al. (1999) A six-stranded double-psi β-barrel is shared by several protein superfamilies. Structure 7:227-236.
    • (1999) Structure , vol.7 , pp. 227-236
    • Castillo, R.M.1
  • 11
    • 0028838717 scopus 로고
    • Threading a database of protein cores
    • Madej T, Gibrat JF, Bryant SH (1995) Threading a database of protein cores. Proteins 23:356-369.
    • (1995) Proteins , vol.23 , pp. 356-369
    • Madej, T.1    Gibrat, J.F.2    Bryant, S.H.3
  • 12
    • 0034819564 scopus 로고    scopus 로고
    • Grass group I pollen allergens (β-expansins) lack proteinase activity and do not cause wall loosening via proteolysis
    • Li LC, Cosgrove DJ (2001) Grass group I pollen allergens (β-expansins) lack proteinase activity and do not cause wall loosening via proteolysis. Eur J Biochem 268:4217-4226.
    • (2001) Eur J Biochem , vol.268 , pp. 4217-4226
    • Li, L.C.1    Cosgrove, D.J.2
  • 13
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in 3 dimensions
    • Krissinel E, Henrick K (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in 3 dimensions. Acta Crystallogr D 60:2256-2268.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 14
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D 60:2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 15
    • 0026666191 scopus 로고
    • Three-dimensional structure in solution of barwin, a protein from barley seed
    • Ludvigsen S, Poulsen FM (1992) Three-dimensional structure in solution of barwin, a protein from barley seed. Biochemistry 31:8783-8789.
    • (1992) Biochemistry , vol.31 , pp. 8783-8789
    • Ludvigsen, S.1    Poulsen, F.M.2
  • 16
    • 0028822343 scopus 로고
    • Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9 A resolution
    • Davies GJ, Tolley SP, Henrissat B, Hjort C, Schulein M (1995) Structures of oligosaccharide-bound forms of the endoglucanase V from Humicola insolens at 1.9 A resolution. Biochemistry 34:16210-16220.
    • (1995) Biochemistry , vol.34 , pp. 16210-16220
    • Davies, G.J.1    Tolley, S.P.2    Henrissat, B.3    Hjort, C.4    Schulein, M.5
  • 17
    • 25444435724 scopus 로고    scopus 로고
    • Model cellulose films exposed to H. insolens glucoside hydrolase family 45 endocellulase: The effect of the carbohydrate-binding module
    • Eriksson J, et al. (2005) Model cellulose films exposed to H. insolens glucoside hydrolase family 45 endocellulase: The effect of the carbohydrate-binding module. J Colloid Interface Sci 285:94-99.
    • (2005) J Colloid Interface Sci , vol.285 , pp. 94-99
    • Eriksson, J.1
  • 18
    • 0037616181 scopus 로고    scopus 로고
    • Crystal structure of a family 45 endoglucanase from Melanocarpus albomyces: Mechanistic implications based on the free and cellobiose-bound forms
    • Hirvonen M, Papageorgiou AC (2003) Crystal structure of a family 45 endoglucanase from Melanocarpus albomyces: Mechanistic implications based on the free and cellobiose-bound forms. J Mol Biol 329:403-410.
    • (2003) J Mol Biol , vol.329 , pp. 403-410
    • Hirvonen, M.1    Papageorgiou, A.C.2
  • 19
    • 0035140936 scopus 로고    scopus 로고
    • Identification of four families of peptidoglycan lytic transglycosylases
    • Blackburn NT, Clarke AJ (2001) Identification of four families of peptidoglycan lytic transglycosylases. J Mol Evol 52:78-84.
    • (2001) J Mol Evol , vol.52 , pp. 78-84
    • Blackburn, N.T.1    Clarke, A.J.2
  • 20
    • 24944507285 scopus 로고    scopus 로고
    • Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold
    • van Straaten KE, Dijkstra BW, Vollmer W, Thunnissen AM (2005) Crystal structure of MltA from Escherichia coli reveals a unique lytic transglycosylase fold. J Mol Biol 352:1068-1080.
    • (2005) J Mol Biol , vol.352 , pp. 1068-1080
    • van Straaten, K.E.1    Dijkstra, B.W.2    Vollmer, W.3    Thunnissen, A.M.4
  • 21
    • 34547138663 scopus 로고    scopus 로고
    • Structure of Escherichia coli lytic transglycosylase MltA with bound chitohexaose: Implications for peptidoglycan binding and cleavage
    • van Straaten KE, Barends TR, Dijkstra BW, Thunnissen AM (2007) Structure of Escherichia coli lytic transglycosylase MltA with bound chitohexaose: Implications for peptidoglycan binding and cleavage. J Biol Chem 282:21197-21205.
    • (2007) J Biol Chem , vol.282 , pp. 21197-21205
    • van Straaten, K.E.1    Barends, T.R.2    Dijkstra, B.W.3    Thunnissen, A.M.4
  • 22
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: Fine-tuning polysaccharide recognition
    • Boraston AB, Bolam DN, Gilbert HJ, Davies GJ (2004) Carbohydrate-binding modules: Fine-tuning polysaccharide recognition. Biochem J 382:769-781.
    • (2004) Biochem J , vol.382 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 23
    • 0030960011 scopus 로고    scopus 로고
    • Group I allergens of grass pollen as cell wall-loosening agents
    • Cosgrove DJ, Bedinger P, Durachko DM (1997) Group I allergens of grass pollen as cell wall-loosening agents. Proc Natl Acad Sci USA 94:6559-6564.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6559-6564
    • Cosgrove, D.J.1    Bedinger, P.2    Durachko, D.M.3
  • 24
    • 0034835925 scopus 로고    scopus 로고
    • A fungal endoglucanase with plant cell wall extension activity
    • Yuan S, Wu Y, Cosgrove DJ (2001) A fungal endoglucanase with plant cell wall extension activity. Plant Physiol 127:324-333.
    • (2001) Plant Physiol , vol.127 , pp. 324-333
    • Yuan, S.1    Wu, Y.2    Cosgrove, D.J.3
  • 25
    • 0036953722 scopus 로고    scopus 로고
    • The XTH family of enzymes involved in xyloglucan endotransglucosylation and endohydrolysis: Current perspectives and a new unifying nomenclature
    • Rose JK, Braam J, Fry SC, Nishitani K (2002) The XTH family of enzymes involved in xyloglucan endotransglucosylation and endohydrolysis: Current perspectives and a new unifying nomenclature. Plant Cell Physiol 43:1421-1435.
    • (2002) Plant Cell Physiol , vol.43 , pp. 1421-1435
    • Rose, J.K.1    Braam, J.2    Fry, S.C.3    Nishitani, K.4
  • 26
    • 0023514772 scopus 로고
    • The functions of autolysins in the growth and division of Bacillus subtilis
    • Doyle RJ, Koch AL (1987) The functions of autolysins in the growth and division of Bacillus subtilis. Crit Rev Microbiol 15:169-222.
    • (1987) Crit Rev Microbiol , vol.15 , pp. 169-222
    • Doyle, R.J.1    Koch, A.L.2
  • 27
    • 0019452877 scopus 로고
    • The energized membrane and cellular autolysis in Bacillus subtilis
    • Jolliffe LK, Doyle RJ, Streips UN (1981) The energized membrane and cellular autolysis in Bacillus subtilis. Cell 25:753-763.
    • (1981) Cell , vol.25 , pp. 753-763
    • Jolliffe, L.K.1    Doyle, R.J.2    Streips, U.N.3
  • 28
    • 20444369856 scopus 로고    scopus 로고
    • Biocontrol of Bacillus subtilis against Fusarium verticillioides in vitro and at the maize root level
    • Cavaglieri L, Orlando J, Rodriguez MI, Chulze S, Etcheverry M (2005) Biocontrol of Bacillus subtilis against Fusarium verticillioides in vitro and at the maize root level. Res Microbiol 156:748-754.
    • (2005) Res Microbiol , vol.156 , pp. 748-754
    • Cavaglieri, L.1    Orlando, J.2    Rodriguez, M.I.3    Chulze, S.4    Etcheverry, M.5
  • 29
    • 0344688136 scopus 로고    scopus 로고
    • Clavibacter michiganensis subsp michiganensis: First steps in the understanding of virulence of a Gram-positive phytopathogenic bacterium
    • Gartemann KH, et al. (2003) Clavibacter michiganensis subsp michiganensis: First steps in the understanding of virulence of a Gram-positive phytopathogenic bacterium. J Biotechnol 106:179-191.
    • (2003) J Biotechnol , vol.106 , pp. 179-191
    • Gartemann, K.H.1
  • 30
    • 0034517720 scopus 로고    scopus 로고
    • The cellulase encoded by the native plasmid of Clavibacter michiganensis ssp sepedonicus plays a role in virulence and contains an expansin-like domain
    • Laine MJ, et al. (2000) The cellulase encoded by the native plasmid of Clavibacter michiganensis ssp sepedonicus plays a role in virulence and contains an expansin-like domain. Physiol Mol Plant Pathol 57:221-233.
    • (2000) Physiol Mol Plant Pathol , vol.57 , pp. 221-233
    • Laine, M.J.1
  • 31
    • 48549100257 scopus 로고    scopus 로고
    • Role of swollenin, an expansin-like protein from Trichoderma, in plant root colonization
    • Brotman Y, Briff E, Viterbo A, Chet I (2008) Role of swollenin, an expansin-like protein from Trichoderma, in plant root colonization. Plant Physiol 147:779-789.
    • (2008) Plant Physiol , vol.147 , pp. 779-789
    • Brotman, Y.1    Briff, E.2    Viterbo, A.3    Chet, I.4
  • 32
    • 34250877831 scopus 로고    scopus 로고
    • Plant cell wall degradation by saprophytic Bacillus subtilis strains: Gene clusters responsible for rhamnogalacturonan depolymerization
    • Ochiai A, Itoh T, Kawamata A, Hashimoto W, Murata K (2007) Plant cell wall degradation by saprophytic Bacillus subtilis strains: Gene clusters responsible for rhamnogalacturonan depolymerization. Appl Environ Microbiol 73:3803-3813.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 3803-3813
    • Ochiai, A.1    Itoh, T.2    Kawamata, A.3    Hashimoto, W.4    Murata, K.5
  • 33
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterization and functional significance of transient protein-protein interactions
    • Nooren IM, Thornton JM (2003) Structural characterization and functional significance of transient protein-protein interactions. J Mol Biol 325:991-1018.
    • (2003) J Mol Biol , vol.325 , pp. 991-1018
    • Nooren, I.M.1    Thornton, J.M.2
  • 34
    • 0029106186 scopus 로고
    • Expansin mode of action on cell walls: Analysis of wall hydrolysis, stress relaxation, and binding
    • McQueen-Mason SJ, Cosgrove DJ (1995) Expansin mode of action on cell walls: Analysis of wall hydrolysis, stress relaxation, and binding. Plant Physiol 107:87-100.
    • (1995) Plant Physiol , vol.107 , pp. 87-100
    • McQueen-Mason, S.J.1    Cosgrove, D.J.2
  • 35
    • 0031737309 scopus 로고    scopus 로고
    • A vector for systematic gene inactivation in Bacillus subtilis
    • Vagner V, Dervyn E, Ehrlich SD (1998) A vector for systematic gene inactivation in Bacillus subtilis. Microbiology 144:3097-3104.
    • (1998) Microbiology , vol.144 , pp. 3097-3104
    • Vagner, V.1    Dervyn, E.2    Ehrlich, S.D.3
  • 36
    • 0026955916 scopus 로고
    • Two endogenous proteins that induce cell wall expansion in plants
    • McQueen-Mason S, Durachko DM, Cosgrove DJ (1992) Two endogenous proteins that induce cell wall expansion in plants. Plant Cell 4:1425-1433.
    • (1992) Plant Cell , vol.4 , pp. 1425-1433
    • McQueen-Mason, S.1    Durachko, D.M.2    Cosgrove, D.J.3
  • 37
    • 0041508874 scopus 로고    scopus 로고
    • Purification and characterization of four β-expansins (Zea m 1 isoforms) from maize pollen
    • Li LC, Bedinger PA, Volk C, Jones AD, Cosgrove DJ (2003) Purification and characterization of four β-expansins (Zea m 1 isoforms) from maize pollen. Plant Physiol 132:2073-2085.
    • (2003) Plant Physiol , vol.132 , pp. 2073-2085
    • Li, L.C.1    Bedinger, P.A.2    Volk, C.3    Jones, A.D.4    Cosgrove, D.J.5
  • 38
    • 43549106552 scopus 로고    scopus 로고
    • Assessment of the role of chemotaxis and biofilm formation as requirements for colonization of roots and seeds of soybean plants by Bacillus amyloliquefaciens BNM339
    • Yaryura PM, et al. (2008) Assessment of the role of chemotaxis and biofilm formation as requirements for colonization of roots and seeds of soybean plants by Bacillus amyloliquefaciens BNM339. Curr Microbiol 56:625-632.
    • (2008) Curr Microbiol , vol.56 , pp. 625-632
    • Yaryura, P.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.