Analysis of the Yeast Peptidome and Comparison with the Human Peptidome

• Autor(a) principal: Dasgupta, Sayani
• Data de Publicação: 2016
• Outros Autores: Yang, Ciyu, Castro, Leandro M., Tashima, Alexandre Keiji [UNIFESP], Ferro, Emer S., Moir, Robyn D., Willis, Ian M., Fricker, Lloyd D.
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UNIFESP
• Texto Completo: http://dx.doi.org/10.1371/journal.pone.0163312; https://repositorio.unifesp.br/handle/11600/57098

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