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Volumn 11, Issue 4, 2012, Pages 388-400

Presence of a large β(1-3)glucan linked to chitin at the saccharomyces cerevisiae mother-bud neck suggests involvement in localized growth control

Author keywords

[No Author keywords available]

Indexed keywords

CHITIN; GLUCAN; GLUCAN ENDO 1,3 BETA GLUCOSIDASE; GLYCOSIDASE; SACCHAROMYCES CEREVISIAE PROTEIN; SODIUM HYDROXIDE; SOLVENT;

EID: 84859146267     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.05328-11     Document Type: Article
Times cited : (23)

References (30)
  • 1
    • 0031756531 scopus 로고    scopus 로고
    • A new tool for studying the molecular architecture of the fungal cell wall: One step purification of recombinant Trichoderma β-(1-6)-glucanase expressed in Pichia pastoris
    • Bom IJ, et al. 1998. A new tool for studying the molecular architecture of the fungal cell wall: one step purification of recombinant Trichoderma β-(1-6)-glucanase expressed in Pichia pastoris. Biochim. Biophys. Acta 1425:419-424.
    • (1998) Biochim. Biophys. Acta , vol.1425 , pp. 419-424
    • Bom, I.J.1
  • 2
    • 72449134867 scopus 로고    scopus 로고
    • Two novel techniques for determination of polysaccharide cross-links show that Crh1p and Crh2p attach chitin to both β(1-6)-and β(1-3)glucan in the Saccharomyces cerevisiae cell wall
    • Cabib E. 2009. Two novel techniques for determination of polysaccharide cross-links show that Crh1p and Crh2p attach chitin to both β(1-6)-and β(1-3)glucan in the Saccharomyces cerevisiae cell wall. Eukaryot. Cell 8:1626-1636.
    • (2009) Eukaryot. Cell , vol.8 , pp. 1626-1636
    • Cabib, E.1
  • 3
    • 33846219421 scopus 로고    scopus 로고
    • Crh1p and Crh2p are required for the cross-linking of chitin to β(1-6)glucan in the Saccharomyces cerevisiae cell wall
    • Cabib E, Blanco N, Grau C, Rodríguez-Peña JM, Arroyo J. 2007. Crh1p and Crh2p are required for the cross-linking of chitin to β(1-6)glucan in the Saccharomyces cerevisiae cell wall. Mol. Microbiol. 63:921-935.
    • (2007) Mol. Microbiol. , vol.63 , pp. 921-935
    • Cabib, E.1    Blanco, N.2    Grau, C.3    Rodríguez-Peña, J.M.4    Arroyo, J.5
  • 4
    • 15744368383 scopus 로고    scopus 로고
    • Synthase III-dependent chitin is bound to different acceptors depending on location on the cell wall of budding yeast
    • Cabib E, Durán A. 2005. Synthase III-dependent chitin is bound to different acceptors depending on location on the cell wall of budding yeast. J. Biol. Chem. 280:9170-9179.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9170-9179
    • Cabib, E.1    Durán, A.2
  • 5
    • 0035827639 scopus 로고    scopus 로고
    • The yeast cell wall and septum as paradigms of cell growth and morphogenesis
    • Cabib E, Roh D-H, Schmidt M, Crotti LB, Varma A. 2001. The yeast cell wall and septum as paradigms of cell growth and morphogenesis. J. Biol. Chem. 276:19679-19682.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19679-19682
    • Cabib, E.1    Roh, D.-H.2    Schmidt, M.3    Crotti, L.B.4    Varma, A.5
  • 6
    • 64549158361 scopus 로고    scopus 로고
    • Septins and the lateral compartmentation of eukaryotic membranes
    • Caudron F, Barral Y. 2009. Septins and the lateral compartmentation of eukaryotic membranes. Dev. Cell 16:493-506.
    • (2009) Dev. Cell , vol.16 , pp. 493-506
    • Caudron, F.1    Barral, Y.2
  • 7
    • 0035339523 scopus 로고    scopus 로고
    • Yeast cell permeabilization by osmotic shock allows determination of enzymatic activities in situ
    • Crotti LB, Drgon T, Cabib E. 2001. Yeast cell permeabilization by osmotic shock allows determination of enzymatic activities in situ. Anal. Biochem. 292:8-16.
    • (2001) Anal. Biochem. , vol.292 , pp. 8-16
    • Crotti, L.B.1    Drgon, T.2    Cabib, E.3
  • 8
    • 0033606798 scopus 로고    scopus 로고
    • The GTP-binding protein Rho1p is required for cell cycle progression and polarization of the yeast cell
    • Drgonová J, Drgon T, Roh D-H, Cabib E. 1999. The GTP-binding protein Rho1p is required for cell cycle progression and polarization of the yeast cell. J. Cell Biol. 146:373-387.
    • (1999) J. Cell Biol. , vol.146 , pp. 373-387
    • Drgonová, J.1    Drgon, T.2    Roh, D.-H.3    Cabib, E.4
  • 9
    • 0030844713 scopus 로고    scopus 로고
    • Altered extent of cross-linking of β 1,6-glucosylated mannoproteins to chitin in Saccharomyces cerevisiae mutants with reduced cell wall β 1,3-glucan content
    • Kapteyn JC, et al. 1997. Altered extent of cross-linking of β 1,6-glucosylated mannoproteins to chitin in Saccharomyces cerevisiae mutants with reduced cell wall β 1,3-glucan content. J. Bacteriol. 179:6279-6284.
    • (1997) J. Bacteriol. , vol.179 , pp. 6279-6284
    • Kapteyn, J.C.1
  • 10
    • 0016247209 scopus 로고
    • Lysis of viable yeast cells by enzymes of Arthrobacter luteus. II. Purification and properties of an enzyme, Zymolyase, which lyses viable yeast cells
    • Kitamura K, Kaneko T, Yamamoto Y. 1974. Lysis of viable yeast cells by enzymes of Arthrobacter luteus. II. Purification and properties of an enzyme, Zymolyase, which lyses viable yeast cells. J. Gen. Appl. Microbiol. 20:323-344.
    • (1974) J. Gen. Appl. Microbiol. , vol.20 , pp. 323-344
    • Kitamura, K.1    Kaneko, T.2    Yamamoto, Y.3
  • 11
    • 33645121842 scopus 로고    scopus 로고
    • Cell wall construction in Saccharomyces cerevisiae
    • Klis FM, Boorsma A, De Groot PWJ. 2006. Cell wall construction in Saccharomyces cerevisiae. Yeast 23:185-202.
    • (2006) Yeast , vol.23 , pp. 185-202
    • Klis, F.M.1    Boorsma, A.2    de Groot, P.W.J.3
  • 12
    • 0028897101 scopus 로고
    • Architecture of the yeast cell wall. The linkage between chitin and β (1→3)-glucan
    • Kollár R, Petráková E, Ashwell G, Robbins PW, Cabib E. 1995. Architecture of the yeast cell wall. The linkage between chitin and β (1→3)-glucan. J. Biol. Chem. 270:1170-1178.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1170-1178
    • Kollár, R.1    Petráková, E.2    Ashwell, G.3    Robbins, P.W.4    Cabib, E.5
  • 13
    • 0030814079 scopus 로고    scopus 로고
    • Architecture of the yeast cell wall. β (1→6)-Glucan interconnects mannoprotein, β(1→3)-glucan, and chitin
    • Kollár R, et al. 1997. Architecture of the yeast cell wall. β (1→6)-Glucan interconnects mannoprotein, β(1→3)-glucan, and chitin. J. Biol. Chem. 272:17762-17775.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17762-17775
    • Kollár, R.1
  • 14
    • 0016273444 scopus 로고
    • Demonstration of a fibrillar component in the cell wall of the yeast Saccharomyces cerevisiae and its chemical nature
    • Kopecká M, Phaff HG, Fleet GH. 1974. Demonstration of a fibrillar component in the cell wall of the yeast Saccharomyces cerevisiae and its chemical nature. J. Cell Biol. 62:66-76.
    • (1974) J. Cell Biol. , vol.62 , pp. 66-76
    • Kopecká, M.1    Phaff, H.G.2    Fleet, G.H.3
  • 15
    • 33645120423 scopus 로고    scopus 로고
    • Cell wall assembly in Saccharomyces cerevisiae
    • Lesage G, Bussey H. 2006. Cell wall assembly in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 70:317-343.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 317-343
    • Lesage, G.1    Bussey, H.2
  • 16
    • 0032567760 scopus 로고    scopus 로고
    • Sequential assembly of myosin II, an IQGAP-like protein, and filamentous actin to a ring structure involved in budding yeast cytokinesis
    • Lippincott J, Li R. 1998. Sequential assembly of myosin II, an IQGAP-like protein, and filamentous actin to a ring structure involved in budding yeast cytokinesis. J. Cell Biol. 140:355-366.
    • (1998) J. Cell Biol. , vol.140 , pp. 355-366
    • Lippincott, J.1    Li, R.2
  • 17
    • 0036468065 scopus 로고    scopus 로고
    • A refined method for the determination of Saccharomyces cerevisiae cell wall composition and β-1,6-glucan fine structure
    • Magnelli P, Cipollo JF, Abeijón C. 2002. A refined method for the determination of Saccharomyces cerevisiae cell wall composition and β-1,6-glucan fine structure. Anal. Biochem. 301:136-150.
    • (2002) Anal. Biochem. , vol.301 , pp. 136-150
    • Magnelli, P.1    Cipollo, J.F.2    Abeijón, C.3
  • 18
    • 0015822017 scopus 로고
    • The structure of a β-(1→3)-D-glucan from yeast cell walls
    • Manners DJ, Masson AJ, Patterson JC. 1973. The structure of a β-(1→3)-D-glucan from yeast cell walls. Biochem. J. 135:19-30.
    • (1973) Biochem. J. , vol.135 , pp. 19-30
    • Manners, D.J.1    Masson, A.J.2    Patterson, J.C.3
  • 19
    • 0023135564 scopus 로고
    • Linkages between glucosaminoglycan and glucan determine alkali-insolubility of the glucan in walls of Saccharomyces cerevisiae
    • Mol PC, Wessels JGH. 1987. Linkages between glucosaminoglycan and glucan determine alkali-insolubility of the glucan in walls of Saccharomyces cerevisiae. FEMS Microbiol. Lett. 41:95-99.
    • (1987) FEMS Microbiol. Lett. , vol.41 , pp. 95-99
    • Mol, P.C.1    Wessels, J.G.H.2
  • 20
    • 0034685921 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored glucanosyltransferases play an active role in the biosynthesis of the fungal cell wall
    • Mouyna I, et al. 2000. Glycosylphosphatidylinositol-anchored glucanosyltransferases play an active role in the biosynthesis of the fungal cell wall. J. Biol. Chem. 275:14882-14889.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14882-14889
    • Mouyna, I.1
  • 21
    • 0031027101 scopus 로고    scopus 로고
    • Increase in chitin as an essential response to defects in assembly of cell wall polymers in the ggp1Δ mutant of Saccharomyces cerevisiae
    • Popolo L, Gilardelli D, Bonfante P, Vai M. 1997. Increase in chitin as an essential response to defects in assembly of cell wall polymers in the ggp1Δ mutant of Saccharomyces cerevisiae. J. Bacteriol. 179:463-469.
    • (1997) J. Bacteriol. , vol.179 , pp. 463-469
    • Popolo, L.1    Gilardelli, D.2    Bonfante, P.3    Vai, M.4
  • 22
    • 0020392369 scopus 로고
    • Serratia marcescens chitinase: One-step purification and use for the determination of chitin
    • Roberts RL, Cabib E. 1982. Serratia marcescens chitinase: one-step purification and use for the determination of chitin. Anal. Biochem. 127:402-412.
    • (1982) Anal. Biochem. , vol.127 , pp. 402-412
    • Roberts, R.L.1    Cabib, E.2
  • 23
    • 0342748465 scopus 로고    scopus 로고
    • A novel family of cell wall-related proteins regulated differentially during the yeast life cycle
    • Rodríguez-Peña JM, Cid VJ, Arroyo J, Nombela C. 2000. A novel family of cell wall-related proteins regulated differentially during the yeast life cycle. Mol. Cell. Biol. 20:3245-3255.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3245-3255
    • Rodríguez-Peña, J.M.1    Cid, V.J.2    Arroyo, J.3    Nombela, C.4
  • 24
    • 0037096167 scopus 로고    scopus 로고
    • Mechanisms for targeting of the Saccharomyces cerevisiae GPIanchored cell wall protein Crh2p to polarized growth sites
    • Rodríguez-Peña JM, Rodríguez C, Alvarez A, Nombela C, Arroyo J. 2002. Mechanisms for targeting of the Saccharomyces cerevisiae GPIanchored cell wall protein Crh2p to polarized growth sites. J. Cell Sci. 115:2549-2558.
    • (2002) J. Cell Sci. , vol.115 , pp. 2549-2558
    • Rodríguez-Peña, J.M.1    Rodríguez, C.2    Alvarez, A.3    Nombela, C.4    Arroyo, J.5
  • 25
    • 73949120734 scopus 로고    scopus 로고
    • Immobilization of the glycosylphosphatidylinositolanchored Gas1 protein into the chitin ring and septum is required for proper morphogenesis in yeast
    • Rolli E, et al. 2009. Immobilization of the glycosylphosphatidylinositolanchored Gas1 protein into the chitin ring and septum is required for proper morphogenesis in yeast. Mol. Biol. Cell 20:4856-4870.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4856-4870
    • Rolli, E.1
  • 26
    • 0037081643 scopus 로고    scopus 로고
    • In budding yeast, contraction of the actomyosin ring and formation of the primary septum at cytokinesis depend on each other
    • Schmidt M, Bowers B, Varma A, Roh D-H, Cabib E. 2002. In budding yeast, contraction of the actomyosin ring and formation of the primary septum at cytokinesis depend on each other. J. Cell Sci. 115:293-302.
    • (2002) J. Cell Sci. , vol.115 , pp. 293-302
    • Schmidt, M.1    Bowers, B.2    Varma, A.3    Roh, D.-H.4    Cabib, E.5
  • 27
    • 0037910282 scopus 로고    scopus 로고
    • Septins, under Cla4p regulation, and the chitin ring are required for neck integrity in budding yeast
    • Schmidt M, Varma A, Drgon T, Bowers B, Cabib E. 2003. Septins, under Cla4p regulation, and the chitin ring are required for neck integrity in budding yeast. Mol. Biol. Cell 14:2128-2141.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2128-2141
    • Schmidt, M.1    Varma, A.2    Drgon, T.3    Bowers, B.4    Cabib, E.5
  • 28
    • 0026058639 scopus 로고
    • The function of chitin synthases 2 and 3 in the Saccharomyces cerevisiae cell cycle
    • Shaw JA, et al. 1991. The function of chitin synthases 2 and 3 in the Saccharomyces cerevisiae cell cycle. J. Cell Biol. 114:111-123.
    • (1991) J. Cell Biol. , vol.114 , pp. 111-123
    • Shaw, J.A.1
  • 29
    • 0024669291 scopus 로고
    • A system of shuttle vectors and host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski R, Hieter P. 1989. A system of shuttle vectors and host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-28.
    • (1989) Genetics , vol.122 , pp. 19-28
    • Sikorski, R.1    Hieter, P.2
  • 30
    • 76949125280 scopus 로고
    • Studies on yeast metabolism 1. Fractionation and microdetermination of cell carbohydrates
    • Trevelyan WE, Harrison JS. 1952. Studies on yeast metabolism 1. Fractionation and microdetermination of cell carbohydrates. Biochem. J. 50: 298-303.
    • (1952) Biochem. J. , vol.50 , pp. 298-303
    • Trevelyan, W.E.1    Harrison, J.S.2


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