Journal of Bacteriology, April 2001, p. 2273-2279, Vol. 183, No. 7
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.7.2273-2279.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Unité des Aspergillus, Institut Pasteur, Paris,1 and Infectious Disease Group, Biochemistry Department2 and Central Research Functions, Biophysics Department,3 Hoechst Marion Roussel, Romainville, France
Received 26 October 2000/Accepted 15 January 2001
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 was achieved in Escherichia coli. Anti-Fks1p
antibodies labeled the apex of the germ tube, as did aniline blue
fluorochrome, which was specific for
(1-3) glucans, showing that
AfFks1p colocalized with the newly synthesized
(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 H+-ATPase, and a 160-kDa protein
which was labeled by an anti-
(1-3) glucan antibody and was
homologous to ABC bacterial
(1-2) glucan transporters.
Present address: Swammerdam Institute for Life Science, University
of Amsterdam, Amsterdam, The Netherlands.
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