PXD010827-1

PXD010827 is an original dataset announced via ProteomeXchange.

Title	Genetic analysis of Hsp70 phosphorylation sitesreveals a role in Candida albicanscell and colony morphogenesis
Description	Heat shock proteins are best known for their role as chaperonins involved in general proteostasis, but they can also participate in specific cellular regulatory pathways, e.g. via their post-translational modification. Hsp70/Ssa1 is a central cytoplasmic chaperonin in eukaryotes, which also participates in cell cycle regulation via its phosphorylation at a specific residue. Here we analyze the role of Ssa1 phosphorylation in the morphogenesis of the fungus Candida albicans, a common human opportunistic pathogen. C. albicans can assume alternative yeast and hyphal (mold) morphologies, an ability that contributes to its virulence. We identified 11 phosphorylation sites on C. albicans Ssa1, of which 8were only detected in the hyphalcells. Genetic analysis of these sites revealedallele-specific effects on growth at high temperature, cell and colony morphology, and resistance to cell wall-active drugs.This analysis could help direct screens for Ssa1-specific drugs to combat C. albicans virulence.The pleiotropic effects of many Ssa1 mutations are consistent with the large number of Ssa1 client proteins, whereas the lack of concordance between the phenotypes of the different alleles suggests that different sites on Ssa1 can affect interaction with specific classes of client protein, and that modification of these sites can play cellular regulatory roles, consistent with the “chaperone code” hypothesis.
HostingRepository	PRIDE
AnnounceDate	2018-11-21
AnnouncementXML	Submission_2018-11-21_05:15:50.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD010827
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Donald Wolfgeher
SpeciesList	scientific name: Candida albicans (Yeast); NCBI TaxID: 5476;
ModificationList	Ammonia-loss; Phospho; Formyl; Dehydrated; Oxidation; Acetyl; Carbamidomethyl
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2018-08-20 02:57:00	ID requested
⏵ 1	2018-11-21 05:15:51	announced
2	2018-12-04 03:58:44	announced	Updated project metadata.
3	2019-03-11 14:33:29	announced	Updated project metadata.
4	2023-11-14 08:49:56	announced	2023-11-14: Updated project metadata.

Dataset with its publication pending

submitter keyword: Candida albicans, colony morphology, Hsp70, post-translational modification, mass spectrometry, Q-Exactive, LFQ Quantification.

Dr. Daniel Kornitzer
contact affiliation	Department of Molecular Microbiology, B. Rappaport Faculty of Medicine, Technion – I.I.T. and the Rappaport Institute for Research in the Medical Sciences, Haifa 31096, Israel
contact email	danielk@technion.ac.il
lab head
Donald Wolfgeher
contact affiliation	University of Chicago
contact email	donw@uchicago.edu
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD010827
     1. Label: PRIDE project
     2. Name: Genetic analysis of Hsp70 phosphorylation sitesreveals a role in Candida albicanscell and colony morphogenesis