Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Sequential fractionation and two-dimensional gel analysis unravels the complexity of the dimorphic fungus Candida albicans cell wall proteome.
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The abstract supports a C. albicans cell-wall proteomic workflow but does not expose the peptide-level HSP104 evidence.
"Mass spectrometry analyses have allowed the identification of several cell surface proteins classically associated with both the cell wall and other compartments."
The [PSI+] prion of Saccharomyces cerevisiae can be propagated by an Hsp104 orthologue from Candida albicans.
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C. albicans CaHsp104 is a stress-inducible Hsp104 ortholog that complements S. cerevisiae hsp104 for high-temperature tolerance, heat-denatured protein reactivation, and PSI+ prion propagation.
"CaHsp104 is able to provide all known functions of ScHsp104 in an S. cerevisiae hsp104 null mutant, i.e., tolerance to high-temperature stress, reactivation of heat-denatured proteins, and propagation of the [PSI+] prion."
Identification of sumoylation targets, combined with inactivation of SMT3, reveals the impact of sumoylation upon growth, morphology, and stress resistance in the pathogen Candida albicans.
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Hsp104 is a C. albicans sumoylation target, and mutating its consensus SUMO site affected thermal-stress resistance.
"Mutation of consensus sumoylation sites in Hsp60 and Hsp104 affected the resistance of C. albicans to thermal stress."
The heat-induced molecular disaggregase Hsp104 of Candida albicans plays a role in biofilm formation and pathogenicity in a worm infection model.
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C. albicans hsp104/hsp104 mutants are heat sensitive, and HSP104 reintegration restores thermotolerance.
"Mutants lacking HSP104 became hypersusceptible to lethally high temperatures, similarly to the corresponding mutants of Saccharomyces cerevisiae, whereas normal susceptibility was restored upon reintroduction of the gene."
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HSP104 expression before lethal heat shock is sufficient to confer extra thermal protection.
"Turning on expression of HSP104 prior to administration of the heat shock resulted in cells acquiring a greater thermotolerance with respect to cells of the wild-type strain"
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HSP104 loss impairs mature C. albicans biofilm formation on abiotic surfaces.
"biofilm formation by cells lacking HSP104 proved to be defective in two established in vitro models that use polystyrene and polyurethane as the substrates."
Crystal structures of Hsp104 N-terminal domains from Saccharomyces cerevisiae and Candida albicans suggest the mechanism for the function of Hsp104 in dissolving prions.
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The Candida Hsp104 N-terminal domain has a conserved putative peptide-binding groove in the structural region used by Hsp104 to engage misfolded clients.
"The structures of ScHsp104NTD and CaHsp104NTD reveal that the yeast Hsp104 NTD may utilize a conserved putative peptide-binding groove to interact with misfolded polypeptides."