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Journal of Bacteriology, January 2000, p. 320-326, Vol. 182, No. 2
Instituto de Investigaciones
Biomédicas "Alberto Sols," Consejo Superior de
Investigaciones Científicas-UAM, Unidad de
Bioquímica y Genética de Levaduras, 28029 Madrid, Spain
Received 7 July 1999/Accepted 25 October 1999
We have cloned a Candida albicans gene
(CaMIG1) that encodes a protein homologous to the
DNA-binding protein Mig1 from Saccharomyces cerevisiae (ScMig1). The C. albicans Mig1
protein (CaMig1) differs from ScMig1, in that,
among other things, it lacks a putative phosphorylation site for Snf1
and presents several long stretches rich in glutamine or in
asparagine, serine, and threonine and has the effector domain located
at some distance (50 amino acids) from the carboxy terminus. Expression
of CaMIG1 was low and was similar in glucose-, sucrose-, or
ethanol-containing media. Disruption of the two CaMIG1
genomic copies had no effect in filamentation or infectivity. Levels of
a glucose-repressible
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Isolation of the MIG1 Gene from
Candida albicans and Effects of Its Disruption on
Catabolite Repression
-glucosidase, implicated in both sucrose and
maltose utilization, were similar in wild-type or mig1/mig1
cells. Disruption of CaMIG1 had also no effect on the
expression of the glucose-repressed gene CaGAL1. CaMIG1 was
functional in S. cerevisiae, as judged by its ability to
suppress the phenotypes produced by mig1 or
tps1 mutations. In addition, CaMig1 formed
specific complexes with the URS1 region of the S. cerevisiae
FBP1 gene. The existence of a possible functional analogue of
CaMIG1 in C. albicans was suggested by the
results of band shift experiments.
*
Corresponding author. Mailing address: Instituto
de Investigaciones Biomédicas, C/Arturo Duperier no. 4, E-28029 Madrid, Spain. Phone: 34-91-5854620. Fax: 34-91-5854587. E-mail: cgancedo{at}iib.uam.es.
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