scholarly journals Retraction for Chavez-Dozal et al. Functional Analysis of the Exocyst Subunit Sec15 in Candida albicans

2015 ◽  
Vol 14 (12) ◽  
pp. ii-ii ◽  
Author(s):  
Alba A. Chavez-Dozal ◽  
Stella M. Bernardo ◽  
Hallie S. Rane ◽  
Samuel A. Lee
Keyword(s):  
Functional Analysis ◽  
Candida Albicans

The Candida albicans plasma membrane protein Rch1p, a member of the vertebrate SLC10 carrier family, is a novel regulator of cytosolic Ca2+ homoeostasis

2012 ◽  
Vol 444 (3) ◽  
pp. 497-502 ◽  
Author(s):  
Linghuo Jiang ◽  
Joerg Alber ◽  
Jihong Wang ◽  
Wei Du ◽  
Xuexue Yang ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Candida Albicans ◽  
Plasma Membrane ◽  
Membrane Protein ◽  
Solute Carrier Family ◽  
Plasma Membrane Protein ◽  
Cellular Functions ◽  
Downstream Target ◽  
Solute Carrier ◽  
High Concentrations

Candida albicans RCH1 (regulator of Ca2+ homoeostasis 1) encodes a protein of ten TM (transmembrane) domains, homologous with human SLC10A7 (solute carrier family 10 member 7), and Rch1p localizes in the plasma membrane. Deletion of RCH1 confers hypersensitivity to high concentrations of extracellular Ca2+ and tolerance to azoles and Li+, which phenocopies the deletion of CaPMC1 (C. albicans PMC1) encoding the vacuolar Ca2+ pump. Additive to CaPMC1 mutation, lack of RCH1 alone shows an increase in Ca2+ sensitivity, Ca2+ uptake and cytosolic Ca2+ level. The Ca2+ hypersensitivity is abolished by cyclosporin A and magnesium. In addition, deletion of RCH1 elevates the expression of CaUTR2 (C. albicans UTR2), a downstream target of the Ca2+/calcineurin signalling. Mutational and functional analysis indicates that the Rch1p TM8 domain, but not the TM9 and TM10 domains, are required for its protein stability, cellular functions and subcellular localization. Therefore Rch1p is a novel regulator of cytosolic Ca2+ homoeostasis, which expands the functional spectrum of the vertebrate SLC10 family.

scholarly journals Phosphomannosylation and the Functional Analysis of the Extended Candida albicans MNN4-Like Gene Family

2017 ◽  
Vol 8 ◽  
Author(s):  
Roberto J. González-Hernández ◽  
Kai Jin ◽  
Marco J. Hernández-Chávez ◽  
Diana F. Díaz-Jiménez ◽  
Elías Trujillo-Esquivel ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Candida Albicans ◽  
Gene Family

scholarly journals Conservation of the Prion Properties of Ure2p through Evolution

2003 ◽  
Vol 14 (8) ◽  
pp. 3449-3458 ◽  
Author(s):  
Agnès Baudin-Baillieu ◽  
Eric Fernandez-Bellot ◽  
Fabienne Reine ◽  
Eric Coissac ◽  
Christophe Cullin
Keyword(s):  
Functional Analysis ◽  
Candida Albicans ◽  
Gene Deletion ◽  
Yeast Species ◽  
Kluyveromyces Lactis ◽  
In Silico Analysis ◽  
Functional Domain ◽  
Extreme Situation ◽  
Homologous Genes ◽  
Silico Analysis

The yeast inheritable [URE3] element corresponds to a prion form of the nitrogen catabolism regulator Ure2p. We have isolated several orthologous URE2 genes in different yeast species: Saccharomyces paradoxus, S. uvarum, Kluyveromyces lactis, Candida albicans, and Schizosaccharomyces pombe. We show here by in silico analysis that the GST-like functional domain and the prion domain of the Ure2 proteins have diverged separately, the functional domain being more conserved through the evolution. The more extreme situation is found in the two S. pombe genes, in which the prion domain is absent. The functional analysis demonstrates that all the homologous genes except for the two S. pombe genes are able to complement the URE2 gene deletion in a S. cerevisiae strain. We show that in the two most closely related yeast species to S. cerevisiae, i.e., S. paradoxus and S. uvarum, the prion domains of the proteins have retained the capability to induce [URE3] in a S. cerevisiae strain. However, only the S. uvarum full-length Ure2p is able to behave as a prion. We also show that the prion inactivation mechanisms can be cross-transmitted between the S. cerevisiae and S. uvarum prions.

Functional analysis of CaRAP1 , encoding the Repressor/activator protein 1 of Candida albicans

Gene ◽  
2003 ◽  
Vol 307 ◽  
pp. 151-158 ◽  
Author(s):  
Kajal Biswas ◽  
Klaus-Jörg Rieger ◽  
Joachim Morschhäuser
Keyword(s):  
Functional Analysis ◽  
Candida Albicans ◽  
Activator Protein 1 ◽  
Activator Protein

scholarly journals Molecular and functional analysis of the LYS1 gene of Candida albicans.

1994 ◽  
Vol 62 (11) ◽  
pp. 5027-5031 ◽  
Author(s):  
R Garrad ◽  
T M Schmidt ◽  
J K Bhattacharjee
Keyword(s):  
Functional Analysis ◽  
Candida Albicans

scholarly journals A functional analysis of the Als5, Als6 and Als7 genes of Candida albicans

2002 ◽  
Vol 6 ◽  
pp. S52-S53
Author(s):  
D.C. Sheppard ◽  
A.S. Ibrahim ◽  
Y. Fu ◽  
S.G. Filler ◽  
J.E. Edwards
Keyword(s):  
Functional Analysis ◽  
Candida Albicans

scholarly journals Functional Analysis of CaIPT1, a Sphingolipid Biosynthetic Gene Involved in Multidrug Resistance and Morphogenesis of Candida albicans

2005 ◽  
Vol 49 (8) ◽  
pp. 3442-3452 ◽  
Author(s):  
Tulika Prasad ◽  
Preeti Saini ◽  
Naseem Akhtar Gaur ◽  
Ram A. Vishwakarma ◽  
Luqman Ahmad Khan ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Candida Albicans ◽  
Fluorescent Protein ◽  
Efflux Pump ◽  
Major Facilitator Superfamily ◽  
Phospholipid Content ◽  
Specific Substrate ◽  
Biosynthetic Gene ◽  
Surface Localization ◽  
Mutant Cells

ABSTRACT In the present study we describe the isolation and functional analysis of a sphingolipid biosynthetic gene, IPT1, of Candida albicans. The functional consequence of the disruption of both alleles of IPT1 was confirmed by mass analysis of its sphingolipid composition. The disruption of both alleles or a single allele of IPT1 did not lead to any change in growth phenotype or total sphingolipid, ergosterol, or phospholipid content of the mutant cells. The loss of mannosyl diinositol diphosphoceramide [M(IP)2C] in the ipt1 disruptant, however, resulted in increased sensitivity to drugs like 4-nitroquinoline oxide, terbinafine, o-phenanthroline, fluconazole, itraconazole, and ketoconazole. The increase in drug susceptibilities of ipt1 cells was linked to an altered sphingolipid composition, which appeared to be due to the impaired functionality of Cdr1p, a major drug efflux pump of C. albicans that belongs to the ATP binding cassette superfamily. Our confocal and Western blotting results demonstrated that surface localization of green fluorescent protein-tagged Cdr1p was affected in ipt1 disruptant cells. Poor surface localization of Cdr1p resulted in an impaired ability to efflux fluconazole and rhodamine 6G. The effect of mannosyl inositol phosphoceramide accumulation in the ipt1 mutant and the absence of M(IP)2C from the ipt1 mutant on the efflux of drug substrates was very selective. The efflux of methotrexate, a specific substrate of CaMdr1p, another major efflux pump of major facilitator superfamily, remained unaffected in ipt1 mutant cells. Interestingly, changes in sphingolipid composition affected the ability of mutant cells to form proper hyphae in various media. Taken together, our results demonstrate that an altered composition of sphingolipid, which is among the major constituents of membrane rafts, affects the drug susceptibilities and morphogenesis of C. albicans.

scholarly journals Single-Molecule Imaging and Functional Analysis of Als Adhesins and Mannans during Candida albicans Morphogenesis

ACS Nano ◽  
2012 ◽  
Vol 6 (12) ◽  
pp. 10950-10964 ◽  
Author(s):  
Audrey Beaussart ◽  
David Alsteens ◽  
Sofiane El-Kirat-Chatel ◽  
Peter N. Lipke ◽  
Sona Kucharíková ◽  
...  
Keyword(s):  
Functional Analysis ◽  
Candida Albicans ◽  
Single Molecule ◽  
Single Molecule Imaging
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