Escherichia coli is one of the most widely used hosts for the production of heterologous
proteins and its genetics are far better characterized than those of any other microorganism …

Heat shock proteins 90 (Hsp90) and 70 (Hsp70) are two families of highly conserved ATP-
dependent molecular chaperones that fold and remodel proteins. Both are important …

We systematically analyzed the capability of the major cytosolic chaperones of Escherichia
coli to cope with protein misfolding and aggregation during heat stress in vivo and in cell …

SUMMARY α-Crystallins were originally recognized as proteins contributing to the
transparency of the mammalian eye lens. Subsequently, they have been found in many, but …

Small heat shock proteins (sHsps) can efficiently prevent the aggregation of unfolded
proteins in vitro. However, how this in vitro activity translates to function in vivo is poorly …

Publisher Summary The goal of this chapter is to clarify the diversity within the heat shock
proteins (sHsps) family and to describe evidence indicating that sHsps have many different …

The relevance of molecular mechanisms governing mitochondrial proteostasis to the
differentiation and function of hematopoietic and immune cells is largely elusive. Through …

ClpB is a heat-shock protein fromEscherichia coli with an unknown function. We studied a
possible molecular chaperone activity of ClpB in vitro. Firefly luciferase was denatured in …

Summary The Hsp100/Clp ATPases constitute a family of closely related proteins of which
some members function solely as chaperones whereas others additionally can associate …

We investigated the roles of chaperones and proteases in quality control of proteins in the
Escherichia coli cytosol. In ΔrpoH mutants, which lack the heat shock transcription factor and …