Envelope biogenesis and homeostasis in gram-negative bacteria are exceptionally intricate
processes that require a multitude of periplasmic chaperones to ensure cellular survival …

The folding of proteins into their native structure is crucial for the functioning of all biological
processes. Molecular chaperones are guardians of the proteome that assist in protein …

Hsp90s are ATP-dependent chaperones that collaborate with co-chaperones and Hsp70s to
remodel client proteins. Grp94 is the ER Hsp90 homolog essential for folding multiple …

ATP-independent chaperones like trigger factor are generally assumed to play passive roles
in protein folding by acting as holding chaperones. Here we show that trigger factor plays a …

Some misfolded protein conformations can bypass proteostasis machinery and remain
soluble in vivo. This is an unexpected observation, as cellular quality control mechanisms …

The major classes of molecular chaperones have highly variable sequences, sizes, and
shapes, yet they all bind to unfolded proteins, limit their aggregation, and assist in their …

Periplasmic proteins are involved in a wide range of bacterial functions, including motility,
biofilm formation, sensing environmental cues, and small-molecule transport. In addition, a …

Maintaining the health of the proteome is a critical cellular task. Recently, we found G-
quadruplex (G4) nucleic acids are especially potent at preventing protein aggregation in …

Molecular chaperones, a family of proteins of which Hsp90 and Hsp70 are integral
members, form an essential machinery to maintain healthy proteomes by controlling the …

ATP-independent chaperones are usually considered to be holdases that rapidly bind to
non-native states of substrate proteins and prevent their aggregation. These chaperones are …