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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Analysis of the Yeast Peptidome and Comparison with the Human Peptidome

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Autor(es):
Dasgupta, Sayani ; Yang, Ciyu ; Castro, Leandro M. ; Tashima, Alexandre K. ; Ferro, Emer S. ; Moir, Robyn D. ; Willis, Ian M. ; Fricker, Lloyd D.
Número total de Autores: 8
Tipo de documento: Artigo Científico
Fonte: PLoS One; v. 11, n. 9 SEP 29 2016.
Citações Web of Science: 7
Resumo

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. (AU)

Processo FAPESP: 12/19321-9 - Caracterização proteômica e peptidômica dos venenos de aranhas brasileiras por espectrometria de massas
Beneficiário:Alexandre Keiji Tashima
Linha de fomento: Auxílio à Pesquisa - Regular