Activation of Degp Chaperone-Protease Via Formation of Large Activation of Degp Chaperone-Protease Via Formation of Large Cage-Like Oligomers Upon Binding To Substrate Proteins Cage-Like Oligomers Upon Binding To Substrate Proteins

Navigating the oligomeric landscape of the periplasmic stress response protease-chaperone DegP with charge detection mass spectrometry

Charge detection mass spectrometry (CDMS) is applied to directly measure the masses of individual DegP ions, resolving the complete oligomeric distribution in the absence and presence of four clients of increasing size and further establishes CDMS as a powerful single-molecule tool for dissecting heterogeneous protein...

Identification of a Ubiquitin-Independent Degron by a Reporter Assay.

Experimental strategies to identify UID degrons that mediate degradation by the catalytic 20S proteasome particle are described and an integrated workflow-spanning degron mapping to functional validation-provides a generalizable framework for uncovering ubiquitin-independent degrons.

Production of membrane-embedded Bcl-2 proteins - Use of cell-free synthesis in continuous exchange for co-translational insertion of Bcl-2 proteins in lipid bilayer nanodiscs

Structural and Functional Diversity of Serine Protease-Like DEG (Degradation of periplasmic proteins) Genes in Potato (Solanum tuberosum L.)

A comprehensive genome-wide analysis identified 19 serine protease-like DEG family proteins in potato, revealing their structural diversity, domain architecture, and regulatory potential and highlighting the functional versatility of DEG proteases in potato development and stress adaptation.

Adaptability of the GroEL/GroES chaperonin to proteostatic challenge revealed by directed evolution.

The folding of newly synthesized proteins is assisted by an essential network of proteins known as molecular chaperones. In bacteria, the chaperones Trigger Factor (TF), DnaK/DnaJ (Hsp70 system), and GroEL/GroES (chaperonin system) are key players in proteostasis maintenance. Here, we further explore the cooperation an...

Chaperone structure is not a sufficient determinant for the hierarchy of substrate secretion in bacterial type III secretion systems

It is shown that the gene linkage of SscB and SseF is critical for these proteins’ stability and SseF secretion and that chaperone structure is not a sufficient molecular determinant for the correct order of substrate secretion.