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Identifying the mechanisms of eukaryotic genome evolution by comparative genomics is often complicated by the multiplicity of events that have taken place throughout the history of individual lineages, leaving only distorted and superimposed traces in the genome of each living organism. The hemiascomycete yeasts, with their compact genomes, similar(More)
Following endoplasmic reticulum (ER) stress, eukaryotic cells trigger a conserved signal transduction pathway called the unfolded protein response (UPR) that regulates the ER's capacity to perform protein folding according to cellular demand. In Saccharomyces cerevisiae, the UPR is initiated by Ire1, a type I transmembrane serine/threonine(More)
Since its description by Fields and Song in 1989 (Nature 340, 245-246), the yeast two-hybrid system has been used extensively to study protein-protein interactions, becoming increasingly efficient with technological and methodological improvements. Here, we report the construction of a highly representative two-hybrid genomic library for the dimorphic yeast(More)
The yeast Yarrowia lipolytica is a model organism for in vivo study of the signal recognition particle-dependent targeting pathway. In this report, we defined solubilization conditions and set up a fractionation procedure of Y. lipolytica microsomes to determine the amounts of Sec61p-containing translocation pores linked to ribosomes. In contrast to(More)
Cell wall proteins are central to the virulence of Candida albicans. Hwp1, Hwp2 and Rbt1 form a family of hypha-associated cell surface proteins. Hwp1 and Hwp2 have been involved in adhesion and other virulence traits but Rbt1 is still poorly characterized. To assess the role of Rbt1 in the interaction of C. albicans with biotic and abiotic surfaces(More)
Signal recognition particle-dependent targeting of secretory proteins to the endoplasmic reticulum membrane is predominant in the yeast Yarrowia lipolytica. A conditional lethal mutant of the SCR2-encoded 7S RNA provided the first in vivo evidence for involvement of this particle in cotranslational translocation (He, F., Beckerich, J. M., and Gaillardin, C.(More)
The cell wall of Candida albicans is composed of mannoproteins associated to glycan polymers. Most of these proteins are retained in this compartment through a phosphodiester linkage between a remnant of their glycosylphosphatidylinositol anchor and the beta-1,6-glucan polymer. A pure beta-1,6-glucanase is thus required in order to release them. In this(More)
Candida albicans is an opportunistic pathogen. It adheres to mammalian cells through a variety of adhesins that interact with host ligands. The spatial organization of these adhesins on the cellular interface is however poorly understood, mainly because of the lack of an instrument able to track single molecules on single cells. In this context, the atomic(More)
Glycosylphosphatidylinositol (GPI)-anchored proteins are an important class of cell wall proteins in Candida albicans because of their localization and their function, even if more than half of them have no characterized homolog in the databases. In this study, we focused on the IFF protein family, investigating their exposure on the cell surface and the(More)
Twenty-two strains of Corynebacterium pseudotuberculosis, the causative agent of caseous lymphadenitis, were isolated from typical abscesses in sheep and goats from flocks in 6 different regions of France and were characterized. These strains were uniform in biochemical characteristics, susceptibility to 8 antimicrobial agents, and virulence for OF1 mice.(More)