The social and structural architecture of the yeast protein interactome.
Journal
Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462
Informations de publication
Date de publication:
Dec 2023
Dec 2023
Historique:
received:
18
11
2022
accepted:
11
10
2023
medline:
11
12
2023
pubmed:
16
11
2023
entrez:
15
11
2023
Statut:
ppublish
Résumé
Cellular functions are mediated by protein-protein interactions, and mapping the interactome provides fundamental insights into biological systems. Affinity purification coupled to mass spectrometry is an ideal tool for such mapping, but it has been difficult to identify low copy number complexes, membrane complexes and complexes that are disrupted by protein tagging. As a result, our current knowledge of the interactome is far from complete, and assessing the reliability of reported interactions is challenging. Here we develop a sensitive high-throughput method using highly reproducible affinity enrichment coupled to mass spectrometry combined with a quantitative two-dimensional analysis strategy to comprehensively map the interactome of Saccharomyces cerevisiae. Thousand-fold reduced volumes in 96-well format enabled replicate analysis of the endogenous GFP-tagged library covering the entire expressed yeast proteome
Identifiants
pubmed: 37968396
doi: 10.1038/s41586-023-06739-5
pii: 10.1038/s41586-023-06739-5
pmc: PMC10700138
doi:
Substances chimiques
Fungal Proteins
0
Proteome
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
192-200Informations de copyright
© 2023. The Author(s).
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