Analysis of the Yeast Peptidome and Comparison with the Human Peptidome
Proteome
Two-hybrid screening
DOI:
10.1371/journal.pone.0163312
Publication Date:
2016-09-29T14:33:36Z
AUTHORS (8)
ABSTRACT
Peptides function as signaling molecules in species diverse humans and yeast. Mass spectrometry-based peptidomics techniques provide a relatively unbiased method to assess the peptidome of biological samples. In present study, we used quantitative peptidomic technique characterize yeast Saccharomyces cerevisiae compare it peptidomes mammalian cell lines tissues. Altogether, 297 peptides derived from 75 proteins were identified. The are similar those human average size amino acid composition. Inhibition proteasome activity with either bortezomib or epoxomicin led decreased levels some peptides, suggesting that these generated by proteasome. Approximately 30% correspond N- C-terminus protein; is also highly represented C-terminal protein fragments. Most subset abundant proteins, many functions involving cellular metabolism synthesis folding. Of give rise 24 have orthologs and/or mouse for some, same region found human, mouse, peptidomes. Taken together, results support hypothesis intracellular may specific conserved functions.
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