Dynamic 3D proteomes reveal protein functional alterations at high resolution in situ.

ABSTRACT: Biological processes are regulated by intermolecular interactions and chemical modifications that do not affect protein levels, thus escaping detection in classical proteomic screens. We demonstrate here that a global protein structural readout based on limited proteolysis-mass spectrometry (LiP-MS) detects many such functional alterations, simultaneously and in situ, in bacteria undergoing nutrient adaptation and in yeast responding to acute stress. The structural readout, visualized as structural barcodes, captured enzyme activity changes, phosphorylation, protein aggregation, and complex formation, with the resolution of individual regulated functional sites such as binding and active sites. Comparison with prior knowledge, including other 'omics data, showed that LiP-MS detects many kn

SUBMITTER: Cappelletti V 

PROVIDER: S-EPMC7836100 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature