A 1,3-β-glucanosyltransferase isolated from the cell wall of Aspergillus fumigatus is a homologue of the yeast Bgl2p

被引：77

作者：

Mouyna, I

Hartland, RP

Fontaine, T

Diaquin, M

Simenel, C

Delepierre, M

Henrissat, B

Latgé, JP

机构：

[1] Inst Pasteur, Lab Aspergillus, F-75015 Paris, France

[2] Inst Pasteur, Lab Resonance Magnet Nucl, F-75015 Paris, France

[3] CNRS, IFR1, F-13402 Marseille 20, France

来源：

MICROBIOLOGY-SGM | 1998年 / 144卷

关键词：

Aspergillus fumigatus; BGT1; cell wall; 1,3-beta-glucan; BGL2;

D O I：

10.1099/00221287-144-11-3171

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

A 1,3-beta-gtucanosyltransferase which introduces intrachain 1,6-beta linkages into 1,3-beta-glucan was isolated from the cell wall of Aspergillus fumigatus. The biochemical and molecular characterization of the A. fumigatus transferase showed it was homologous to the Saccharomyces cerevisiae and Candida albicans transferase Bg12p. A null mutant constructed in A. fumigatus by gene replacement did not show a distinct phenotype from the parental strain. The putative function of this major cell-wail-associated protein is discussed.

引用

页码：3171 / 3180

页数：10

共 46 条

[21] BETA-GLUCOSIDASE, BETA-GALACTOSIDASE, FAMILY-A CELLULASES, FAMILY-F XYLANASES AND 2 BARLEY GLYCANASES FORM A SUPERFAMILY OF ENZYMES WITH 8-FOLD BETA/ALPHA-ARCHITECTURE AND WITH 2 CONSERVED GLUTAMATES NEAR THE CARBOXY-TERMINAL ENDS OF BETA-STRAND-4 AND BETA-STRAND-7 [J].