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Scw10p, a cell-wall glucanase/transglucosidase important for cell-wall stability in Saccharomyces cerevisiae

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Veröffentlicht in: Microbiology 150(2004), 10, Seite 3197-3208
Personen und Körperschaften: Sestak, Sergej (VerfasserIn), Strahl, Sabine (VerfasserIn)
Titel: Scw10p, a cell-wall glucanase/transglucosidase important for cell-wall stability in Saccharomyces cerevisiae/ Sergej Sestak, Ilja Hagen, Widmar Tanner and Sabine Strahl
Format: E-Book-Kapitel
Sprache: Englisch
veröffentlicht:
01/10/2004
Gesamtaufnahme: : Microbiology, 150(2004), 10, Seite 3197-3208
, volume:150
Quelle: Verbunddaten SWB
Lizenzfreie Online-Ressourcen
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contents Glycosyl hydrolases and transferases are crucial for the formation of a rigid but at the same time plastic cell wall in yeasts and fungi. The Saccharomyces cerevisiae glucan hydrolase family 17 (GH17) contains the soluble cell-wall proteins Scw4p, Scw10p, Scw11p and Bgl2p. For Bgl2p, endoglucanase/glucanosyltransferase activity has been demonstrated, and Scw11p has been shown to be involved in cell separation. Here, Scw4p and Scw10p, which show 63% amino acid identity, were characterized. scw4 and scw10 single mutants were sensitive towards cell-wall destabilizing agents, suggesting a role in cell-wall assembly or maintenance. Simultaneous deletion of SCW4 and SCW10 showed a synergistic effect, and activated the cell-wall compensatory mechanism in a PKC1-dependent manner. Both the amount of cell-wall chitin and the amount of mannoproteins attached to chitin were increased in mutant scw4scw10. Deletion of CHS3 proved the critical role of chitin in scw4scw10. However, the mannoprotein Sed1p and the glucan synthase Fks2p were also crucial for cell-wall stability in mutant scw4scw10. The exchange of two conserved glutamate residues localized in the putative catalytic domain of GH17 family members strongly suggests that Scw10p acts as a 1,3-β-glucanase or as a 1,3-β-glucanosyltransferase. In addition, the synthetic interactions between Bgl2p and Scw10p which support a functional cooperation in cell-wall assembly were analysed. The data suggest that Scw4p and Scw10p act as glucanases or transglucosidases in concert with other cell-wall proteins to assure cell-wall integrity.
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spelling Sestak, Sergej VerfasserIn aut, Scw10p, a cell-wall glucanase/transglucosidase important for cell-wall stability in Saccharomyces cerevisiae Sergej Sestak, Ilja Hagen, Widmar Tanner and Sabine Strahl, 01/10/2004, 12, Text txt rdacontent, Computermedien c rdamedia, Online-Ressource cr rdacarrier, Gesehen am 11.05.2017, Glycosyl hydrolases and transferases are crucial for the formation of a rigid but at the same time plastic cell wall in yeasts and fungi. The Saccharomyces cerevisiae glucan hydrolase family 17 (GH17) contains the soluble cell-wall proteins Scw4p, Scw10p, Scw11p and Bgl2p. For Bgl2p, endoglucanase/glucanosyltransferase activity has been demonstrated, and Scw11p has been shown to be involved in cell separation. Here, Scw4p and Scw10p, which show 63% amino acid identity, were characterized. scw4 and scw10 single mutants were sensitive towards cell-wall destabilizing agents, suggesting a role in cell-wall assembly or maintenance. Simultaneous deletion of SCW4 and SCW10 showed a synergistic effect, and activated the cell-wall compensatory mechanism in a PKC1-dependent manner. Both the amount of cell-wall chitin and the amount of mannoproteins attached to chitin were increased in mutant scw4scw10. Deletion of CHS3 proved the critical role of chitin in scw4scw10. However, the mannoprotein Sed1p and the glucan synthase Fks2p were also crucial for cell-wall stability in mutant scw4scw10. The exchange of two conserved glutamate residues localized in the putative catalytic domain of GH17 family members strongly suggests that Scw10p acts as a 1,3-β-glucanase or as a 1,3-β-glucanosyltransferase. In addition, the synthetic interactions between Bgl2p and Scw10p which support a functional cooperation in cell-wall assembly were analysed. The data suggest that Scw4p and Scw10p act as glucanases or transglucosidases in concert with other cell-wall proteins to assure cell-wall integrity., Strahl, Sabine VerfasserIn (DE-588)1034793055 (DE-627)74629073X (DE-576)382427939 aut, Enthalten in Microbiology Reading : Soc., 1947 150(2004), 10, Seite 3197-3208 Online-Ressource (DE-627)318884879 (DE-600)2008736-6 (DE-576)090894154 1465-2080 nnns, volume:150 year:2004 number:10 pages:3197-3208 extent:12, http://dx.doi.org/10.1099/mic.0.27293-0 Verlag Resolving-System kostenfrei Volltext, http://mic.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.27293-0 Verlag kostenfrei Volltext, http://dx.doi.org/10.1099/mic.0.27293-0 LFER, LFER 2017-06-08T00:00:00Z
spellingShingle Sestak, Sergej, Strahl, Sabine, Scw10p, a cell-wall glucanase/transglucosidase important for cell-wall stability in Saccharomyces cerevisiae, Glycosyl hydrolases and transferases are crucial for the formation of a rigid but at the same time plastic cell wall in yeasts and fungi. The Saccharomyces cerevisiae glucan hydrolase family 17 (GH17) contains the soluble cell-wall proteins Scw4p, Scw10p, Scw11p and Bgl2p. For Bgl2p, endoglucanase/glucanosyltransferase activity has been demonstrated, and Scw11p has been shown to be involved in cell separation. Here, Scw4p and Scw10p, which show 63% amino acid identity, were characterized. scw4 and scw10 single mutants were sensitive towards cell-wall destabilizing agents, suggesting a role in cell-wall assembly or maintenance. Simultaneous deletion of SCW4 and SCW10 showed a synergistic effect, and activated the cell-wall compensatory mechanism in a PKC1-dependent manner. Both the amount of cell-wall chitin and the amount of mannoproteins attached to chitin were increased in mutant scw4scw10. Deletion of CHS3 proved the critical role of chitin in scw4scw10. However, the mannoprotein Sed1p and the glucan synthase Fks2p were also crucial for cell-wall stability in mutant scw4scw10. The exchange of two conserved glutamate residues localized in the putative catalytic domain of GH17 family members strongly suggests that Scw10p acts as a 1,3-β-glucanase or as a 1,3-β-glucanosyltransferase. In addition, the synthetic interactions between Bgl2p and Scw10p which support a functional cooperation in cell-wall assembly were analysed. The data suggest that Scw4p and Scw10p act as glucanases or transglucosidases in concert with other cell-wall proteins to assure cell-wall integrity.
swb_id_str 488532051
title Scw10p, a cell-wall glucanase/transglucosidase important for cell-wall stability in Saccharomyces cerevisiae
title_auth Scw10p, a cell-wall glucanase/transglucosidase important for cell-wall stability in Saccharomyces cerevisiae
title_full Scw10p, a cell-wall glucanase/transglucosidase important for cell-wall stability in Saccharomyces cerevisiae Sergej Sestak, Ilja Hagen, Widmar Tanner and Sabine Strahl
title_fullStr Scw10p, a cell-wall glucanase/transglucosidase important for cell-wall stability in Saccharomyces cerevisiae Sergej Sestak, Ilja Hagen, Widmar Tanner and Sabine Strahl
title_full_unstemmed Scw10p, a cell-wall glucanase/transglucosidase important for cell-wall stability in Saccharomyces cerevisiae Sergej Sestak, Ilja Hagen, Widmar Tanner and Sabine Strahl
title_in_hierarchy Scw10p, a cell-wall glucanase/transglucosidase important for cell-wall stability in Saccharomyces cerevisiae / Sergej Sestak, Ilja Hagen, Widmar Tanner and Sabine Strahl,
title_short Scw10p, a cell-wall glucanase/transglucosidase important for cell-wall stability in Saccharomyces cerevisiae
title_sort scw10p a cell wall glucanase transglucosidase important for cell wall stability in saccharomyces cerevisiae
url http://dx.doi.org/10.1099/mic.0.27293-0, http://mic.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.27293-0