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pmid:26608260

Quantitative differential proteomics of yeast extracellular matrix: there is more to it than meets the eye.

Fábio Faria-Oliveira · Joana Carvalho · Célia Ferreira · Maria Luisa Hernáez · Concha Gil · Cândida Lucas

BMC microbiology · 2015 doi:10.1186/s12866-015-0550-1

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Experiment

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Data

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Analysis

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Record details sci_version · id · kind · revision · content_hash · schema · created_at · updated_at · generator
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pmid:26608260
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science-record
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2026-11-01T15:40:14Z
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paper object · 10 fields
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title
Quantitative differential proteomics of yeast extracellular matrix: there is more to it than meets the eye.
doi
10.1186/s12866-015-0550-1
pmid
26608260
authors array · 6 items
[0]
Fábio Faria-Oliveira
[1]
Joana Carvalho
[2]
Célia Ferreira
[3]
Maria Luisa Hernáez
[4]
Concha Gil
[5]
Cândida Lucas
journal
BMC microbiology
year
2015
abstract
BACKGROUND: Saccharomyces cerevisiae multicellular communities are sustained by a scaffolding extracellular matrix, which provides spatial organization, and nutrient and water availability, and ensures group survival. According to this tissue-like biology, the yeast extracellular matrix (yECM) is analogous to the higher Eukaryotes counterpart for its polysaccharide and proteinaceous nature. Few works focused on yeast biofilms, identifying the flocculin Flo11 and several members of the HSP70 in the extracellular space. Molecular composition of the yECM, is therefore mostly unknown. The homologue of yeast Gup1 protein in high Eukaryotes (HHATL) acts as a regulator of Hedgehog signal secretion, therefore interfering in morphogenesis and cell-cell communication through the ECM, which mediates but is also regulated by this signalling pathway. In yeast, the deletion of GUP1 was associated with a vast number of diverse phenotypes including the cellular differentiation that accompanies biofilm formation. METHODS: S. cerevisiae W303-1A wt strain and gup1∆ mutant were used as previously described to generate biofilm-like mats in YPDa from which the yECM proteome was extracted. The proteome from extracellular medium from batch liquid growing cultures was used as control for yECM-only secreted proteins. Proteins were separated by SDS-PAGE and 2DE. Identification was performed by HPLC, LC-MS/MS and MALDI-TOF/TOF. The protein expression comparison between the two strains was done by DIGE, and analysed by DeCyder Extended Data Analysis that included Principal Component Analysis and Hierarchical Cluster Analysis. RESULTS: The proteome of S. cerevisiae yECM from biofilm-like mats was purified and analysed by Nano LC-MS/MS, 2D Difference Gel Electrophoresis (DIGE), and MALDI-TOF/TOF. Two strains were compared, wild type and the mutant defective in GUP1. As controls for the identification of the yECM-only proteins, the proteome from liquid batch cultures was also identified. Proteins were grouped into distinct functional classes, mostly Metabolism, Protein Fate/Remodelling and Cell Rescue and Defence mechanisms, standing out the presence of heat shock chaperones, metalloproteinases, broad signalling cross-talkers and other putative signalling proteins. The data has been deposited to the ProteomeXchange with identifier PXD001133. CONCLUSIONS: yECM, as the mammalian counterpart, emerges as highly proteinaceous. As in higher Eukaryotes ECM, numerous proteins that could allow dynamic remodelling, and signalling events to occur in/and via yECM were identified. Importantly, large sets of enzymes encompassing full antagonistic metabolic pathways, suggest that mats develop into two metabolically distinct populations, suggesting that either extensive moonlighting or actual metabolism occurs extracellularly. The gup1∆ showed abnormally loose ECM texture. Accordingly, the correspondent differences in proteome unveiled acetic and citric acid producing enzymes as putative players in structural integrity maintenance.
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Comparisons between wt and gup1Δ mutant were carried out using average ratio and unpaired Student’s t-test.
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Comparisons between wt and gup1Δ mutant were carried out using average ratio and unpaired Student’s t-test.
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The full lists of yECM and LGM proteins from both strains were deposited in the ProteomeXchange database - identifier PXD001133.
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Proteome of Saccharomyces cerevisiae extracellular matrix
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Quantitative differential proteomics of yeast extracellular matrix: there is more
[1]
d 2DE. Identification was performed by HPLC, LC-MS/MS and MALDI-TOF/TOF. The protein expression co
[2]
-like mats was purified and analysed by Nano LC-MS/MS, 2D Difference Gel Electrophoresis (DIGE), a
[3]
cerevisiae wt and ∆gup1 ECM proteome by Nano LC-MS/MS Compared analysis of wt and ∆gup1 yECM prote
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Principal Component Analysis
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Complete file
{"sci_version": "1.2", "schema": "https://corpus.bntrg.co.uk/sci/1.0/sci.schema.json", "id": "pmid:26608260", "kind": "science-record", "revision": 6, "content_hash": "sha256:c1091060c5d7d39be8c82c850d4ce38dbbd84f79e1c45ba0bad6ef80c8cd935b", "created_at": "2026-11-01T15:40:14Z", "updated_at": "2026-11-01T21:20:17Z", "generator": {"name": "corpus-assay-engine", "run_id": "reading-sci-2026-11-01"}, "paper": {"state": "complete", "title": "Quantitative differential proteomics of yeast extracellular matrix: there is more to it than meets the eye.", "doi": "10.1186/s12866-015-0550-1", "pmid": "26608260", "authors": ["Fábio Faria-Oliveira", "Joana Carvalho", "Célia Ferreira", "Maria Luisa Hernáez", "Concha Gil", "Cândida Lucas"], "journal": "BMC microbiology", "year": 2015, "abstract": "BACKGROUND: Saccharomyces cerevisiae multicellular communities are sustained by a scaffolding extracellular matrix, which provides spatial organization, and nutrient and water availability, and ensures group survival. According to this tissue-like biology, the yeast extracellular matrix (yECM) is analogous to the higher Eukaryotes counterpart for its polysaccharide and proteinaceous nature. Few works focused on yeast biofilms, identifying the flocculin Flo11 and several members of the HSP70 in the extracellular space. Molecular composition of the yECM, is therefore mostly unknown. The homologue of yeast Gup1 protein in high Eukaryotes (HHATL) acts as a regulator of Hedgehog signal secretion, therefore interfering in morphogenesis and cell-cell communication through the ECM, which mediates but is also regulated by this signalling pathway. In yeast, the deletion of GUP1 was associated with a vast number of diverse phenotypes including the cellular differentiation that accompanies biofilm formation.\nMETHODS: S. cerevisiae W303-1A wt strain and gup1∆ mutant were used as previously described to generate biofilm-like mats in YPDa from which the yECM proteome was extracted. The proteome from extracellular medium from batch liquid growing cultures was used as control for yECM-only secreted proteins. Proteins were separated by SDS-PAGE and 2DE. Identification was performed by HPLC, LC-MS/MS and MALDI-TOF/TOF. The protein expression comparison between the two strains was done by DIGE, and analysed by DeCyder Extended Data Analysis that included Principal Component Analysis and Hierarchical Cluster Analysis.\nRESULTS: The proteome of S. cerevisiae yECM from biofilm-like mats was purified and analysed by Nano LC-MS/MS, 2D Difference Gel Electrophoresis (DIGE), and MALDI-TOF/TOF. Two strains were compared, wild type and the mutant defective in GUP1. As controls for the identification of the yECM-only proteins, the proteome from liquid batch cultures was also identified. Proteins were grouped into distinct functional classes, mostly Metabolism, Protein Fate/Remodelling and Cell Rescue and Defence mechanisms, standing out the presence of heat shock chaperones, metalloproteinases, broad signalling cross-talkers and other putative signalling proteins. The data has been deposited to the ProteomeXchange with identifier PXD001133.\nCONCLUSIONS: yECM, as the mammalian counterpart, emerges as highly proteinaceous. As in higher Eukaryotes ECM, numerous proteins that could allow dynamic remodelling, and signalling events to occur in/and via yECM were identified. Importantly, large sets of enzymes encompassing full antagonistic metabolic pathways, suggest that mats develop into two metabolically distinct populations, suggesting that either extensive moonlighting or actual metabolism occurs extracellularly. The gup1∆ showed abnormally loose ECM texture. Accordingly, the correspondent differences in proteome unveiled acetic and citric acid producing enzymes as putative players in structural integrity maintenance.", "claims": [{"id": "claim-method", "statement": "Comparisons between wt and gup1Δ mutant were carried out using average ratio and unpaired Student’s t-test.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:26608260", "locator": "sections[19] \"Image acquisition and DIGE analysis\" paragraph 2", "quote": "Comparisons between wt and gup1Δ mutant were carried out using average ratio and unpaired Student’s t-test."}], "state": "complete"}, {"id": "claim-data-access", "statement": "The full lists of yECM and LGM proteins from both strains were deposited in the ProteomeXchange database - identifier PXD001133.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:26608260", "locator": "sections[4] \"Global results\" paragraph 2", "quote": "The full lists of yECM and LGM proteins from both strains were deposited in the ProteomeXchange database - identifier PXD001133."}], "state": "complete"}], "gaps": []}, "experiment": {"state": "complete", "objective": null, "steps": [{"id": "read_published_estimate", "order": 1, "name": "Read the published estimate from the source", "kind": "other", "state": "complete", "blocked_on": null, "description": "The claim, method and evidence span published with the source article.", "duration_hours": null, "parameters": {}, "inputs": ["source:pmid:26608260"], "outputs": ["the published estimate and its evidence"], "instruments": [], "reagents": []}, {"id": "obtain_source_data", "order": 2, "name": "Obtain the source data from the named repository", "kind": "data-preparation", "state": "complete", "blocked_on": null, "description": "The GEO series accession resolves and its sample accessions are listed. This lane did not download the dataset or read its licence.", "duration_hours": null, "parameters": {}, "inputs": ["data:geo:PXD001133"], "outputs": ["the source data with its repository provenance"], "instruments": [], "reagents": []}, {"id": "run_analysis", "order": 3, "name": "Run the published analysis", "kind": "analysis", "state": "complete", "blocked_on": null, "description": "Apply the paper's statistical method to the resolved series and compare the result with the published target.", "duration_hours": null, "parameters": {}, "inputs": ["data:geo:PXD001133"], "outputs": ["the replicated result and its comparison"], "instruments": [], "reagents": []}], "materials": [], "instruments": [], "reagents": [], "conditions": {}, "gaps": []}, "data": {"state": "partial", "assets": [{"id": "source:pmid:26608260", "role": "manuscript", "format": "xml", "media_type": "application/xml", "uri": "https://doi.org/10.1186/s12866-015-0550-1", "sha256": "sha256:81031a00e856c98225fb79d1e57d0b59eefb41bfca2c6f8acd31187b2ef78284", "bytes": 62241, "access": "open", "state": "resolved", "reader": null, "reader_status": "reader_required", "identifier": "10.1186/s12866-015-0550-1", "version": null, "note": "Full article fetched from PMC; the checksum covers the rendered section body, not the original XML bytes.", "structure": {"pmcid": "PMC4660637", "source": "europe_pmc_fulltext", "coverage": "whole_body_without_references", "text_hash_scope": "rendered_section_body"}}, {"id": "data:geo:PXD001133", "role": "raw", "format": "geo-series", "media_type": "application/vnd.ncbi.geo-series+json", "uri": "https://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=PXD001133", "sha256": null, "bytes": null, "access": "open", "state": "resolved", "reader": null, "reader_status": "reader_required", "identifier": "PXD001133", "version": null, "note": "The full lists of yECM and LGM proteins from both strains were deposited in the ProteomeXchange database - identifier PXD001133.", "structure": {"repository": "GEO", "access_route": "GEO accession URL", "access_statement_verbatim": "The full lists of yECM and LGM proteins from both strains were deposited in the ProteomeXchange database - identifier PXD001133.", "access_statement_kind": "data_availability_statement", "sample_accessions": [], "sample_count": null, "group_sizes": null, "group_sizes_basis": null, "platform": null, "taxon": null, "title": "Proteome of Saccharomyces cerevisiae extracellular matrix", "resolution_checked_at": "2026-10-31T18:35:55Z", "resolution_check": "identifier_resolution_only_no_download_no_licence_read", "downloaded": false, "licence_read": false}}, {"id": "asset:table:pmid:26608260:1", "role": "table", "format": "jats-table", "media_type": "application/vnd.jats.table+json", "uri": null, "sha256": "sha256:7e731950c164e161c17e55a17f78942fa59e25db8cd6a5b31fe80e84d53bf435", "bytes": 924, "access": "open", "state": "verified", "reader": "read_table", "reader_status": "available", "identifier": "section[4]/table-wrap[1]#Tab1", "version": null, "note": "Proteins identified applying MALDI-TOF/TOF to the most prominent spots from 2DE", "structure": {"pmcid": "PMC4660637", "section_index": 4, "section_title": "Global results", "row_count": 20, "column_count": 2}, "table": {"label": "Table 1", "caption": "Proteins identified applying MALDI-TOF/TOF to the most prominent spots from 2DE", "rows": [["S. cerevisiae W303 (Wt)"], ["Act1", "Actin 1"], ["Adh1", "Alcohol dehydrogenase 1"], ["Ahp1", "Alkyl hydroperoxide reductase 1"], ["Ald3", "Aldehyde dehydrogenase 3"], ["Cit1", "Citrate synthase 1"], ["Cpr1", "Cyclosporin A-sensitive proline rotamase 1"], ["Eno1", "Enolase 1"], ["Eno2", "Enolase 2"], ["Hsp26", "Heat shock protein 26"], ["Ilv5", "Isoleucine-plus-valine requiring enzyme 5"], ["Oye2", "Old yellow enzyme 2"], ["Pdc1", "Pyruvate decarboxylase 1"], ["Pyk1", "Pyruvate kinase 1"], ["Ree1", "Regulation of Enolase 1"], ["Sod2", "Superoxide dismutase 2"], ["Ssa1", "Stress-seventy subfamily A 1"], ["Tdh3", "Triose-phosphate dehydrogenase 3"], ["Tpi1", "Triose-phosphate isomerase"], ["YNL134C", "Uncharacterized ORF"]], "row_count": 20, "column_count": 2, "numeric_cells": 20, "header_rows": 1, "locator": "section[4]/table-wrap[1]#Tab1"}}, {"id": "asset:table:pmid:26608260:2", "role": "table", "format": "jats-table", "media_type": "application/vnd.jats.table+json", "uri": null, "sha256": "sha256:4ec4b466fdec4d5d2e2ead9c96573817e2540be517ae2c52e00181de1e53f799", "bytes": 343, "access": "open", "state": "verified", "reader": "read_table", "reader_status": "available", "identifier": "section[4]/table-wrap[2]#Tab2", "version": null, "note": "DIGE results: proteins identified in different amounts in the S. cerevisiae wt and gup1∆ mutant yECM. 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