Journal
JOURNAL OF BACTERIOLOGY
Volume 183, Issue 7, Pages 2273-2279Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.183.7.2273-2279.2001
Keywords
-
Categories
Ask authors/readers for more resources
The glucan synthase complex of the human pathogenic mold Aspergillus fumigatus has been investigated. The genes encoding the putative catalytic subunit Fks1p and four Rho proteins of A. fumigatus were cloned and sequenced. Sequence analysis showed that AfFks1p was a transmembrane protein very similar to other Fksp proteins in yeasts and in Aspergillus nidulans. Heterologous expression of the conserved internal hydrophilic domain of AfFks1p aas achieved in Escherichia coli. Anti-Fks1p antibodies labeled the apex of the germ tube, as did aniline blue fluorochrome, which was specific for beta (1-3) glucans, showing that AfFks1p colocalized with the newly synthesized beta (1-3) glucans. AfRHO1, the most homologous gene to RHO1 of Saccharomyces cerevisiae, was studied for the first time in a filamentous fungus. AfRho proteins have GTP binding and hydrolysis consensus sequences identical to those of yeast Rho proteins and have a slightly modified geranylation site in AfRho1p and AfRho3p. Purification of the glucan synthase complex by product entrapment led to the enrichment of four proteins: Fks1p, Rho1p, a 100-kDa protein homologous to a membrane Hf-ATPase, and a 160-kDa protein which was labeled by an anti-beta (13) glucan antibody and was homologous to ABC bacterial beta (1-2) glucan transporters.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available