Analysis of the Yeast Peptidome and Comparison with the Human Peptidome
dc.citation.issue | 9 | |
dc.citation.volume | 11 | |
dc.contributor.author | Dasgupta, Sayani | |
dc.contributor.author | Yang, Ciyu | |
dc.contributor.author | Castro, Leandro M. | |
dc.contributor.author | Tashima, Alexandre Keiji [UNIFESP] | |
dc.contributor.author | Ferro, Emer S. | |
dc.contributor.author | Moir, Robyn D. | |
dc.contributor.author | Willis, Ian M. | |
dc.contributor.author | Fricker, Lloyd D. | |
dc.coverage | San Francisco | |
dc.date.accessioned | 2020-07-31T12:47:48Z | |
dc.date.available | 2020-07-31T12:47:48Z | |
dc.date.issued | 2016 | |
dc.description.abstract | 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 | en |
dc.description.abstract | 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. | en |
dc.description.affiliation | Albert Einstein Coll Med, Dept Mol Pharmacol, Bronx, NY 10461 USA | |
dc.description.affiliation | Mem Sloan Kettering Canc Ctr, Dept Pathol, New York, NY 10065 USA | |
dc.description.affiliation | Sao Paulo State Univ, Inst Biomed Sci, Campus Sao Paulo Coast, BR-11330900 Sao Vicente, SP, Brazil | |
dc.description.affiliation | Univ Fed Sao Paulo, Escola Paulista Med, Dept Biochem, BR-04023901 Sao Paulo, SP, Brazil | |
dc.description.affiliation | Univ Sao Paulo, Inst Biomed Sci, Dept Pharmacol, BR-05508000 Sao Paulo, SP, Brazil | |
dc.description.affiliation | Albert Einstein Coll Med, Dept Biochem, Bronx, NY 10461 USA | |
dc.description.affiliation | Albert Einstein Coll Med, Dept Syst & Computat Biol, Bronx, NY 10461 USA | |
dc.description.affiliation | Albert Einstein Coll Med, Dept Neurosci, Bronx, NY 10461 USA | |
dc.description.affiliationUnifesp | Department of Biochemistry, Escola Paulista de Medicina, Universidade Federal de São Paulo (UNIFESP), Sao Paulo, SP, 04023–901, SP, Brazil | |
dc.description.source | Web of Science | |
dc.description.sponsorship | United States National Institutes of Health [R01-DA004494] | |
dc.description.sponsorship | Brazilian National Research Council [400944/2014-6, 445363/2014-2, 303135/2011-5, 449390/2014-4] | |
dc.description.sponsorship | Financiadora de Estudos e Projetos | |
dc.description.sponsorship | Fundacao de Amparo a Pesquisa do Estado de Sao Paulo [2012/19321-9] | |
dc.description.sponsorshipID | NIH: R01-DA004494 | |
dc.description.sponsorshipID | CNPq: 400944/2014-6 | |
dc.description.sponsorshipID | CNPq: 445363/2014-2 | |
dc.description.sponsorshipID | CNPq: 303135/2011-5 | |
dc.description.sponsorshipID | CNPq: 449390/2014-4 | |
dc.description.sponsorshipID | FAPESP: 2012/19321-9 | |
dc.format.extent | - | |
dc.identifier | http://dx.doi.org/10.1371/journal.pone.0163312 | |
dc.identifier.citation | Plos One. San Francisco, v. 11, n. 9, p. -, 2016. | |
dc.identifier.doi | 10.1371/journal.pone.0163312 | |
dc.identifier.file | WOS000384328500042.pdf | |
dc.identifier.issn | 1932-6203 | |
dc.identifier.uri | https://repositorio.unifesp.br/handle/11600/57098 | |
dc.identifier.wos | WOS:000384328500042 | |
dc.language.iso | eng | |
dc.publisher | Public Library Science | |
dc.relation.ispartof | Plos One | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.title | Analysis of the Yeast Peptidome and Comparison with the Human Peptidome | en |
dc.type | info:eu-repo/semantics/article |
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