Year: 2021
Type: article
Abstract: Protein-protein interactions govern most cellular pathways and processes, and multiple technologies have emerged to systematically map them. Assessing the error of interaction networks has been a challenge. Crosslinking mass spectrometry is currently widening its scope from structural analyses of purified multi-protein complexes towards systems-wide analyses of protein-protein interactions (PPIs). Using a carefully controlled large-scale analysis of Escherichia coli cell lysate, we demonstrate that false-discovery rates (FDR) for PPIs identified by crosslinking mass spectrometry can be reliably estimated. We present an interaction network comprising 590 PPIs at 1% decoy-based PPI-FDR. The structural information included in this network localises the binding site of the hitherto uncharacterised protein YacL to near the DNA exit tunnel on the RNA polymerase.
Source: Nature Communications
Language: English
Subfield: Spectroscopy
Field: Chemistry
Domain: Physical Sciences
Open Access status: gold
Estimated APC paid: $3,721
Awards: G1117759237, Protein structures in the context of time and space by mass spectrometry., EXC 2008: Unifying Systems in Catalysis "UniSysCat", G1659055536, G3606019796, Erfassung der strukturellen Organisation des Mycoplasma pneumoniae Proteoms mittels inZell CrosslinkingMassenspektrometrie, G6637249919, G8136362559, GRK 2473: Bioaktive Peptide Innovative Aspekte zur Synthese und Biosynthese, Core Funding for the Wellcome Trust Centre for Cell Biology
OpenAlex ID: W3166761727