Chaperone Dependency during Primary Protein Biogenesis Does Not Correlate with Chaperone Dependency during <i>in vitro</i> Refolding.

ABSTRACT: Many proteins require molecular chaperones to fold into their functional native forms. Previously we used limited proteolysis mass-spectrometry (LiP-MS) to find that ca. 40% of the E. coli proteome do not efficiently refold spontaneously following dilution from denaturation, a frequency that drops to ca. 15% once molecular chaperones like DnaK or GroEL are provided. However, the roles of chaperones during primary biogenesis in vivo can differ from the functions they play during in vitro refolding experiments. Here, we used LiP-MS to probe structural changes incurred by the E. coli proteome when two key chaperones, trigger factor and DnaKJ, are deleted. While knocking out DnaKJ induces pervasive structural perturbations across the soluble E. coli proteome,

SUBMITTER: Yadav D 

PROVIDER: S-EPMC12224572 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature