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Mapping the O-mannose glycoproteome in Saccharomyces cerevisiae

ABSTRACT: O-Mannosylation is a vital protein modification conserved from fungi to humans. In an essential step towards the full understanding of O-mannosylation we mapped the O mannose glycoproteome in baker´s yeast.

INSTRUMENT(S): Orbitrap Fusion ETD, Orbitrap Fusion

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

TISSUE(S): Haploid Cell

SUBMITTER: Adnan Halim

LAB HEAD: Henrik Clausen

PROVIDER: PXD003238 | Pride | 2016-01-18

REPOSITORIES: Pride

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			Action	DRS
	140814_Fusion_Adnan_Yeast_PN_Trypsin_TCL_ConA010314_2h_LC_2_CID_50_IEF1to12_sub_1xto4xHex.msf	Msf
	140814_Fusion_Adnan_Yeast_PN_Trypsin_TCL_ConA010314_2h_LC_2_ETD_50_IEF1to12.msf	Msf
	140814_Fusion_Adnan_Yeast_PN_Trypsin_TCL_ConA010314_2h_LC_2_HCD_50_IEF1to12.msf	Msf
	140814_Fusion_Adnan_Yeast_PN_Trypsin_TCL_ConA010314_2h_LC_2_HCD_ETD_50_IEF1.raw	Raw
	140814_Fusion_Adnan_Yeast_PN_Trypsin_TCL_ConA010314_2h_LC_2_HCD_ETD_50_IEF10.raw	Raw

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Publications

Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae.

Neubert Patrick P Halim Adnan A Zauser Martin M Essig Andreas A Joshi Hiren J HJ Zatorska Ewa E Larsen Ida Signe Bohse IS Loibl Martin M Castells-Ballester Joan J Aebi Markus M Clausen Henrik H Strahl Sabine S

Molecular & cellular proteomics : MCP 20160113 4

O-Mannosylation is a vital protein modification conserved from fungi to humans. Yeast is a perfect model to study this post-translational modification, because in contrast to mammalsO-mannosylation is the only type ofO-glycosylation. In an essential step toward the full understanding of proteinO-mannosylation we mapped theO-mannose glycoproteome in baker's yeast. Taking advantage of anO-glycan elongation deficient yeast strain to simplify sample complexity, we identified over 500O-glycoproteins ...[more]

PMID: 26764011

Similar Datasets

Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae.

Project description:O-Mannosylation is a vital protein modification conserved from fungi to humans. Yeast is a perfect model to study this post-translational modification, because in contrast to mammalsO-mannosylation is the only type ofO-glycosylation. In an essential step toward the full understanding of proteinO-mannosylation we mapped theO-mannose glycoproteome in baker's yeast. Taking advantage of anO-glycan elongation deficient yeast strain to simplify sample complexity, we identified over 500O-glycoproteins from all subcellular compartments for which over 2300O-mannosylation sites were mapped by electron-transfer dissociation (ETD)-based MS/MS. In this study, we focus on the 293O-glycoproteins (over 1900 glycosylation sites identified by ETD-MS/MS) that enter the secretory pathway and are targets of ER-localized proteinO-mannosyltransferases. We find thatO-mannosylation is not only a prominent modification of cell wall and plasma membrane proteins, but also of a large number of proteins from the secretory pathway with crucial functions in protein glycosylation, folding, quality control, and trafficking. The analysis of glycosylation sites revealed thatO-mannosylation is favored in unstructured regions and β-strands. Furthermore,O-mannosylation is impeded in the proximity ofN-glycosylation sites suggesting the interplay of these types of post-translational modifications. The detailed knowledge of the target proteins and theirO-mannosylation sites opens for discovery of new roles of this essential modification in eukaryotes, and for a first glance on the evolution of different types ofO-glycosylation from yeast to mammals.

| S-EPMC4824858 | biostudies-literature

Mouse kidney Mannose-6-Phosphate Glycoproteome LC-MSMS

Project description:This is the raw data and Byonic search results of mouse kidney Mannose-6-Phosphate glycoproteome.

2020-03-11 | PXD012402 | Pride

Mouse Liver Mannose-6-Phosphate Glycoproteome LC-MSMS

Project description:This is the raw data and Byonic search results of mouse liver Mannose-6-Phosphate glycoproteome.

2020-03-11 | PXD012404 | Pride

Mouse Lung Mannose-6-Phosphate Glycoproteome LC-MSMS

Project description:This is the raw data and Byonic search results of mouse mouse lung Mannose-6-Phosphate glycoproteome.

2020-03-11 | PXD012403 | Pride

Mouse Heart Mannose-6-Phosphate Glycoproteome LC-MSMS

Project description:This is the raw data and Byonic search results of mouse mouse brain Mannose-6-Phosphate glycoproteome.

2020-03-11 | PXD012401 | Pride

Mouse Brain Mannose-6-Phosphate Glycoproteome LC-MSMS

Project description:This is the raw data and Byonic search results of mouse mouse brain Mannose-6-Phosphate glycoproteome.

2020-03-11 | PXD012400 | Pride

Mouse lung N-glycoproteome, phosphoproteome, and M6P glycoproteome

Project description:This is the raw data and Byonic search results of mouse mouse lung N-glycoproteome, phosphoproteome, and Mannose-6-Phosphate glycoproteome.

2022-01-11 | PXD020196 | Pride

Gene expression in a Streptomyces coelicolor strain defective in sco1423 encoding a polyprenol phosphate mannose synthase (Ppm1) compared to the complemented mutant and the wild type parent

Project description:Polyprenol phosphate mannose (PPM) is a lipid linked sugar donor used by extra-cytoplasmic glycosyl tranferases in bacteria. PPM is synthesised by polyprenol phosphate mannose synthase, Ppm1, and in most Actinobacteria is used as the sugar donor for protein O-mannosyl transferase, Pmt, in protein glycosylation. Ppm1 and Pmt have homologues in yeasts and humans, where they are required for protein O-mannosylation. Actinobacteria also use PPM for lipoglycan biosynthesis. Here we show that ppm1 mutants of Streptomyces coelicolor have increased susceptibility to a number of antibiotics that target cell wall biosynthesis. The pmt mutants also have mildly increased antibiotic susceptibilities, in particular to -lactams and vancomycin. Despite normal induction of the vancomycin gene cluster, vanSRJKHAX, the pmt and ppm1 mutants remained highly vancomycin sensitive indicating that the mechanism of resistance is blocked post-transcriptionally. Differential RNA expression analysis indicated that catabolic pathways were downregulated and anabolic ones upregulated in the ppm1 mutant compared to the parent or complemented strains. Of note was the increase in expression of fatty acid biosynthetic genes in the ppm1- mutant. A change in lipid composition was confirmed using Raman spectroscopy, which showed that the ppm1- mutant had a greater relative proportion of unsaturated fatty acids compared to the parent or the complemented mutant. Taken together these data suggest that an inability to synthesise PPM (ppm1-) and loss of the glycoproteome (pmt- mutant) can detrimentally affect membrane or cell envelope functions leading to loss of intrinsic and, in the case of vancomycin, acquired antibiotic resistance.

2018-01-11 | GSE107982 | GEO

Deconstruction of O-glycosylation â€“ Polypeptide GalNAc-T Isoforms Direct Distinct Subsets of the O-Glycoproteome

Project description:GalNAc-transferase (GalNAc-T) isoforms modify distinct subsets of the O-glycoproteome and GalNAc-type O-glycosylation is found on most proteins trafficking through the secretory pathway in metazoan cells. The O-glycoproteome is regulated by up to 20 polypeptide GalNAc-Ts and the contributions and biological functions of individual GalNAc-Ts are poorly understood. Here, we used a zinc-finger nuclease (ZFN)-directed knockout strategy to probe the contributions of the major GalNAc-Ts (GalNAc-T1 and T2) in liver cells, and explore how the GalNAc-T repertoire quantitatively affects the O-glycoproteome. We demonstrate that the majority of the O-glycoproteome is covered by redundancy, whereas distinct subsets of substrates are modified by non-redundant functions of GalNAc-T1 and T2. Differential transcriptomic analysis indicates that loss of function of a GalNAc-T induces specific transcriptional response. The non-redundant O-glycoproteome subsets for and the transcriptional responses for each isoform appeared to be related to different cellular processes, and for the GalNAc-T2 isoform supporting a role in lipid metabolism. The results demonstrate that GalNAc-Ts have non-redundant glycosylation functions, and that these may affect distinct cellular processes. The data provides a comprehensive resource for unique substrates for individual GalNAc-Ts. Our study provides a new view on the regulation of the O-glycoproteome, suggesting that the plurality of GalNAc-Ts arose to regulate distinct protein functions and cellular processes.

2015-09-30 | E-MTAB-3844 | biostudies-arrayexpress

Analysis of intact mannose-6-phosphate glycopeptides

Project description:We have repurposed standard phosphoproteomics workflow based on Fe3+IMAC for enrichment ofmannose-6-phosphate modified glycopeptides. This worklfow was used to profile lysosomal acid hydrolases in HeLa and CHO cell lines. We have combined this approach with CRISPR/Cas9 KO of acid phosphatases 2 and 5 responsible for dephosphorylation of mannose-6-phosphate glycopeptides in the lysosome. This combined approach enabled significantly deeper coverage of CHO mannose-6-phosphate glycoproteome.

2018-12-18 | PXD010333 | Pride

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