This page provides links to various data obtained by the members of the Galar Fungail Consortium. The authors and origin of the data should be acknowledged in any publication that will use this information.
1. Analysis of GPI-anchored proteins in Candida albicans, Saccharomyces cerevisiae, Schizosaccharomyces pombe and Neurospora crassa
These results were pulished in de Groot et al. Yeast 20:780-796 (2003)
These results were pulished in Fradin et al. Mol. Microbiol. 47:1523-1543 (2003).
profiling of Candida albicans strains in blood, in different blood fractions,
and in blood depleted or not of CD15+ cells
These results are provided by A. Brown and coll. (University of Aberdeen, Scotland). They will appear in Garcia-Sanchez, S., Mavor, A., Russel, C. L., Argimon, S., Dennison, P., Enjalbert, B. and Brown, A.J.P. (2005) Global roles of Ssn6 in Tup1- and Nrg1-dependent gene regulation in the fungal pathogen, Candida albicans. Mol. Biol. Cell, in press
7. Transcript profiling of Candida albicans amino acid starvation response (Hélène Tournu, Abigail Mavor, Gwyneth Bertram, and Alistair Brown, Aberdeen University)
This page provides transcript profiling data performed to examine the CaGcn4 and CaGcn2 regulons.
The response to amino acid starvation
(General Amino Acid Control) is a very well characterized mechanism in
the yeast Saccharomyces cerevisiae. It involves the transcription
factor Gcn4, which activates target genes via the responsive element GCRE
in response to amino acid starvation. The regulation of GCN4 activation
is dependent upon four small open reading frames upstream of start codon
in the GCN4 mRNA, which regulate the efficiency and kinetics of
GCN4 translation. Translational Induction of GCN4 involves
the phosphorylation of the initiation factor eIF2a subunit by the Gcn2 protein
kinase. The Candida albicans GCN4 homologue was shown
to mediate a similar response under inducible conditions, and also to
be partly involved in the morphogenetic switch from yeast to pseudohyphal
growth (Tripathi et al. (2002) EMBO Journal 21, 5448-5456).
The C. albicans Gcn2 homologue shares 37% overall identity with
ScGcn2, and 47% identity within the protein kinase domain. Although CaGcn2
is an eIF2a kinase, which phosphorylates
this factor in response to amino acid starvation, strains lacking functional
Gcn2 are resistant to the histidine analogue 3-Aminotriazole (3AT) and
moreover are still capable of initiating the general amino acid response.
data are provided by Hélène Tournu, Abigail Mavor, Gwyneth Bertram, and
Alistair Brown. For additional
information, please contact Alistair Brown (firstname.lastname@example.org).
This work was supported by the EC (QLK2CT-2000-00795),
the Welcome trust (063204),
and the BBSRC (G11780, P10256, P17124).