PXD003916

PXD003916 is an original dataset announced via ProteomeXchange.

Title	Candida albicans is resistant to polyglutamine aggregation and toxicity
Description	Disruption of protein quality control can be detrimental, having toxic effects on single cell organisms, and causing neurodegenerative diseases such as Alzheimer’s, Parkinson’s and Huntington’s in humans. Here we examined the effects of polyQ aggregation in a major fungal pathogen of humans, Candida albicans, with the goal of identifying new approaches to disable this fungus. However, we discovered that expression of poly-glutamine (polyQ) stretches up to 230Q had no effect on C. albicans ability to grow and withstand proteotoxic stress. Bioinformatics analysis demonstrates that C. albicans has a similarly glutamine rich proteome to the unicellular fungus Saccharomyces cerevisiae, which exhibits polyQ toxicity with as few as 72Q. Surprisingly, global transcriptional profiles indicated no significant change upon induction of up to 230Q. Proteomic analysis highlighted two key interactors of 230Q, Sis1 and Sgt2, however, loss of either protein had no additional effect on C. albicans toxicity. Our data suggest that C. albicans has evolved powerful mechanisms to overcome aggregation prone proteins, providing a unique model for studying polyQ associated diseases.
HostingRepository	PRIDE
AnnounceDate	2016-12-06
AnnouncementXML	Submission_2019-02-12_08:06:36.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD003916
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Jonathan Krieger
SpeciesList	scientific name: Candida albicans (Yeast); NCBI TaxID: 5476;
ModificationList	Ammonia-loss; Deamidated; Dehydrated; Oxidation; Acetyl; Carbamidomethyl
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2016-04-06 04:00:11	ID requested
1	2016-12-06 00:41:08	announced
⏵ 2	2019-02-12 08:06:37	announced	Updated publication reference for PubMed record(s): 27807047.

Leach MD, Kim T, DiGregorio SE, Collins C, Zhang Z, Duennwald ML, Cowen LE, Candida albicans Is Resistant to Polyglutamine Aggregation and Toxicity. G3 (Bethesda), 7(1):95-108(2017) [pubmed]

curator keyword: Biomedical

submitter keyword: Candida albicans, toxicity, aggregation, polyQ proteins

Leah E. Cowen
contact affiliation	Department of Molecular Genetics, University of Toronto, Toronto, Ontario, M5S 1A8, Canada.
contact email	leah.cowen@utoronto.ca
lab head
Jonathan Krieger
contact affiliation	SickKids/University of Toronto
contact email	Jonathan.krieger@sickkids.ca
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD003916
     1. Label: PRIDE project
     2. Name: Candida albicans is resistant to polyglutamine aggregation and toxicity