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A map of protein-metabolite interactions reveals principles of chemical communication

ABSTRACT: Application of a novel mass spectrometry-based high-throughput workflow (LiP-SMap) and data resource based on limited proteolysis (LiP) of complex samples. Proteome-wide limited proteolysis sites were obtained in different conditions to infer ligand-induced and protein-protein interaction induced conformational changes. This information was used to identify unknown ligand binding proteins, small molecule-protein binding sites and the remodeling of protein complexes directly in cells.

INSTRUMENT(S): Orbitrap Fusion, Q Exactive Plus, Q Exactive

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

SUBMITTER: Ilaria Piazza

LAB HEAD: Paola Picotti

PROVIDER: PXD006543 | Pride | 2018-01-04

REPOSITORIES: Pride

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	151013_IP581.raw	Raw
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A Map of Protein-Metabolite Interactions Reveals Principles of Chemical Communication.

Piazza Ilaria I Kochanowski Karl K Cappelletti Valentina V Fuhrer Tobias T Noor Elad E Sauer Uwe U Picotti Paola P

Cell 20180104 1-2

Metabolite-protein interactions control a variety of cellular processes, thereby playing a major role in maintaining cellular homeostasis. Metabolites comprise the largest fraction of molecules in cells, but our knowledge of the metabolite-protein interactome lags behind our understanding of protein-protein or protein-DNA interactomes. Here, we present a chemoproteomic workflow for the systematic identification of metabolite-protein interactions directly in their native environment. The approach ...[more]

PMID: 29307493

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