WITHDRAWN: Functional analysis of a gcn5∆/sin3∆ double mutant of Candida albicans coding for a histone acetyltransferase and deacetylase

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

Biochemical Journal ◽

10.1042/bj20112166 ◽

2012 ◽

Vol 444 (3) ◽

pp. 497-502 ◽

Cited By ~ 26

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.

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

Frontiers in Microbiology ◽

10.3389/fmicb.2017.02156 ◽

2017 ◽

Vol 8 ◽

Cited By ~ 9

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

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Conservation of the Prion Properties of Ure2p through Evolution

Molecular Biology of the Cell ◽

10.1091/mbc.e03-01-0007 ◽

2003 ◽

Vol 14 (8) ◽

pp. 3449-3458 ◽

Cited By ~ 48

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.

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

Gene ◽

10.1016/s0378-1119(03)00456-6 ◽

2003 ◽

Vol 307 ◽

pp. 151-158 ◽

Cited By ~ 14

Author(s):

Kajal Biswas ◽

Klaus-Jörg Rieger ◽

Joachim Morschhäuser

Keyword(s):

Functional Analysis ◽

Candida Albicans ◽

Activator Protein 1 ◽

Activator Protein

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Role for Endosomal and Vacuolar GTPases in Candida albicans Pathogenesis

Infection and Immunity ◽

10.1128/iai.01458-08 ◽

2009 ◽

Vol 77 (6) ◽

pp. 2343-2355 ◽

Cited By ~ 26

Author(s):

Douglas A. Johnston ◽

Karen E. Eberle ◽

Joy E. Sturtevant ◽

Glen E. Palmer

Keyword(s):

Candida Albicans ◽

Stress Resistance ◽

Double Mutant ◽

Hyphal Growth ◽

Filamentous Growth ◽

Rab Gtpases ◽

Fungal Cell ◽

Cellular Stresses ◽

Vacuole Biogenesis

ABSTRACT The vacuole has crucial roles in stress resistance and adaptation of the fungal cell. Furthermore, in Candida albicans it has been observed to undergo dramatic expansion during the initiation of hyphal growth, to produce highly “vacuolated” subapical compartments. We hypothesized that these functions may be crucial for survival within the host and tissue-invasive hyphal growth. We also considered the role of the late endosome or prevacuole compartment (PVC), a distinct organelle involved in vacuolar and endocytic trafficking. We identified two Rab GTPases, encoded by VPS21 and YPT72, required for trafficking through the PVC and vacuole biogenesis, respectively. Deletion of VPS21 or YPT72 led to mild sensitivities to some cellular stresses. However, deletion of both genes resulted in a synthetic phenotype with severe sensitivity to cellular stress and impaired growth. Both the vps21Δ and ypt72Δ mutants had defects in filamentous growth, while the double mutant was completely deficient in polarized growth. The defects in hyphal growth were not suppressed by an “active” RIM101 allele or loss of the hyphal repressor encoded by TUP1. In addition, both single mutants had significant attenuation in a mouse model of hematogenously disseminated candidiasis, while the double mutant was rapidly cleared. Histological examination confirmed that the vps21Δ and ypt72Δ mutants are deficient in hyphal growth in vivo. We suggest that the PVC and vacuole are required on two levels during C. albicans infection: (i) stress resistance functions required for survival within tissue and (ii) a role in filamentous growth which may aid host tissue invasion.

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Candida albicans Lacking the Gene Encoding the Regulatory Subunit of Protein Kinase A Displays a Defect in Hyphal Formation and an Altered Localization of the Catalytic Subunit

Eukaryotic Cell ◽

10.1128/ec.3.1.190-199.2004 ◽

2004 ◽

Vol 3 (1) ◽

pp. 190-199 ◽

Cited By ~ 57

Author(s):

Alejandro Cassola ◽

Marc Parrot ◽

Susana Silberstein ◽

Beatrice B. Magee ◽

Susana Passeron ◽

...

Keyword(s):

Candida Albicans ◽

Protein Kinase ◽

Fusion Protein ◽

Protein Kinase A ◽

Double Mutant ◽

Catalytic Subunit ◽

Regulatory Subunit ◽

Wild Type ◽

Gfp Fusion Protein ◽

Kinase A

ABSTRACT The fungal pathogen Candida albicans switches from a yeast-like to a filamentous mode of growth in response to a variety of environmental conditions. We examined the morphogenetic behavior of C. albicans yeast cells lacking the BCY1 gene, which encodes the regulatory subunit of protein kinase A. We cloned the BCY1 gene and generated a bcy1 tpk2 double mutant strain because a homozygous bcy1 mutant in a wild-type genetic background could not be obtained. In the bcy1 tpk2 mutant, protein kinase A activity (due to the presence of the TPK1 gene) was cyclic AMP independent, indicating that the cells harbored an unregulated phosphotransferase activity. This mutant has constitutive protein kinase A activity and displayed a defective germinative phenotype in N-acetylglucosamine and in serum-containing medium. The subcellular localization of a Tpk1-green fluorescent protein (GFP) fusion protein was examined in wild-type, tpk2 null, and bcy1 tpk2 double mutant strains. The fusion protein was observed to be predominantly nuclear in wild-type and tpk2 strains. This was not the case in the bcy1 tpk2 double mutant, where it appeared dispersed throughout the cell. Coimmunoprecipitation of Bcy1p with the Tpk1-GFP fusion protein demonstrated the interaction of these proteins inside the cell. These results suggest that one of the roles of Bcy1p is to tether the protein kinase A catalytic subunit to the nucleus.

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