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Yeast Nuclear Large Scale Cross-linking MS

ABSTRACT: Here, we apply large scale cross-linking mass spectrometry to profile the interactome of isolated and intact Saccharomyces cerevisiae nuclei. Two independent biological replicates (nuclei isolated from different cultures) were performed.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Tara Bartolec

LAB HEAD: Marc R. Wilkins

PROVIDER: PXD014584 | Pride | 2020-03-12

REPOSITORIES: Pride

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Cross-linking Mass Spectrometry Analysis of the Yeast Nucleus Reveals Extensive Protein-Protein Interactions Not Detected by Systematic Two-Hybrid or Affinity Purification-Mass Spectrometry.

Bartolec Tara K TK Smith Daniela-Lee DL Pang Chi Nam Ignatius CNI Xu You Dan YD Hamey Joshua J JJ Wilkins Marc R MR

Analytical chemistry 20200109 2

<i>Saccharomyces cerevisiae</i> has the most comprehensively characterized protein-protein interaction network, or interactome, of any eukaryote. This has predominantly been generated through multiple, systematic studies of protein-protein interactions by two-hybrid techniques and of affinity-purified protein complexes. A pressing question is to understand how large-scale cross-linking mass spectrometry (XL-MS) can confirm and extend this interactome. Here, intact yeast nuclei were subject to cr ...[more]

PMID: 31851481

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