Eukaryotic Cell doi:10.1128/EC.00151-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.
Tcc1p, a novel protein containing the tetratricopeptide repeat motif, interacts with CaTup1p to regulate morphological transition and virulence in Candida albicans
Aki Kaneko,
Takashi Umeyama,
Yuki Utena-Abe,
Satoshi Yamagoe,
Masakazu Niimi,
and
Yoshimasa Uehara*
Department of Bioactive Molecules, National Institute of Infectious Diseases, Tokyo 162-8640, Japan
* To whom correspondence should be addressed. Email:
yuehara{at}nih.go.jp.
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Abstract |
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The transcriptional factor CaTup1p represses many genes involving in intracellular processes including yeast-hyphae transition in the human fungal pathogen Candida albicans. Using tandem affinity purification technology, we identified a novel protein that interacts with CaTup1p, named Tcc1p (Tup1p-complex component). Tcc1p is a C. albicans-specific protein with a 736-amino-acid polypeptide with four tetratricopeptide repeat (TPR) motifs in the N-terminal portion. Tcc1p formed a protein complex with CaTup1p via the TPR domain of Tcc1p, independently of CaSsn6p-CaTup1p. The tcc1
disruptant showed filamentous growth under conditions inducing the yeast form, as true of the Catup1
mutant. Consistent with this result, the common set of hyphae-specific genes was negatively regulated by both TCC1 and CaTUP1. These observations will provide new insights into CaTup1p-dependent transcriptional gene regulation in C. albicans.