PXD004800

PXD004800 is an original dataset announced via ProteomeXchange.

Title	Analysis of the yeast peptidome and comparison with the human peptidome
Description	Peptides function as signaling molecules in species as diverse as humans and yeast. Mass spectrometry-based peptidomics techniques provide a relatively unbiased method to assess the peptidome of biological samples. In the present study, we used a quantitative peptidomic technique to characterize the peptidome of the yeast Saccharomyces cerevisiae and compare it to the peptidomes of mammalian cell lines and tissues. Altogether, 297 yeast peptides derived from 75 proteins were identified. The yeast peptides are similar to those of the human peptidome in average size and amino acid composition. Inhibition of proteasome activity with either bortezomib or epoxomicin led to decreased levels of some yeast peptides, suggesting that these peptides are generated by the proteasome. Approximately 30% of the yeast peptides correspond to the N- or C-terminus of the protein; the human peptidome is also highly represented in N- or C-terminal protein fragments. Most yeast and humans peptides are derived from a subset of abundant proteins, many with functions involving cellular metabolism or protein synthesis and folding. Of the 75 yeast proteins that give rise to peptides, 24 have orthologs that give rise to human and/or mouse peptides and for some, the same region of the proteins are found in the human, mouse, and yeast peptidomes. Taken together, these results support the hypothesis that intracellular peptides may have specific and conserved biological functions.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:06:37.139.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Alexandre Keiji Tashima
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	monohydroxylated residue; acetylated residue
Instrument	Synapt MS

Revision	Datetime	Status	ChangeLog Entry
0	2016-08-15 02:58:04	ID requested
1	2020-06-02 00:41:50	announced
⏵ 2	2024-10-22 05:06:45	announced	2024-10-22: Updated project metadata.

10.1371/journal.pone.0163312;

Dasgupta S, Yang C, Castro LM, Tashima AK, Ferro ES, Moir RD, Willis IM, Fricker LD, Analysis of the Yeast Peptidome and Comparison with the Human Peptidome. PLoS One, 11(9):e0163312(2016) [pubmed]

curator keyword: Biological

submitter keyword: mass spectrometry, Saccharomyces cerevisiae, proteasome,Peptidome

Lloyd D. Fricker
contact affiliation	Department of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, NY 10461, USA
contact email	lloyd.fricker@einstein.yu.edu
lab head
Alexandre Keiji Tashima
contact affiliation	Universidade Federal de Sao Paulo
contact email	aktashima@unifesp.br
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD004800
     1. Label: PRIDE project
     2. Name: Analysis of the yeast peptidome and comparison with the human peptidome