Pulse labeling reveals the tail end of protein folding by proteome profiling.

ABSTRACT: Accurate and efficient folding of nascent protein sequences into their native states requires support from the protein homeostasis network. Herein we probe which newly translated proteins are thermo-sensitive, making them susceptible to misfolding and aggregation under heat stress using pulse-SILAC mass spectrometry. We find a distinct group of proteins that is highly sensitive to this perturbation when newly synthesized but not once matured. These proteins are abundant and highly structured. Notably, they display a tendency to form β sheet secondary structures, have more complex folding topology, and are enriched for chaperone-binding motifs, suggesting a higher demand for chaperone-assisted folding. These polypeptides are also more often components of stable protein complexes in comparis

SUBMITTER: Zhu M 

PROVIDER: S-EPMC9893312 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature