The folding of most newly synthesized proteins in the cell requires the interaction of a variety
of protein cofactors known as molecular chaperones. These molecules recognize and bind …

▪ Abstract A mechanism for regulating gene expression at the level of transcription utilizes an
antagonist of the sigma transcription factor known as the anti-sigma (anti-σ) factor. The …

The glucocorticoid receptor (GR), like many signaling proteins, depends on the Hsp90
molecular chaperone for in vivo function. Although Hsp90 is required for ligand binding in …

Small heat shock proteins (sHsps) are a diverse group of heat-induced proteins that are
conserved in prokaryotes and eukaryotes and are especially abundant in plants. Recent in …

The Escherichia coli Hsp40 DnaJ and Hsp70 DnaK cooperate in the binding of proteins at
intermediate stages of folding, assembly, and translocation across membranes. Binding of …

The ATP-dependent Hsp70s are evolutionary conserved molecular chaperones that
constitute central hubs of the cellular protein quality surveillance network. None of the other …

Proteins of the Hsp70 family of ATPases, such as BiP, function together with J proteins to
bind polypeptides in numerous cellular processes. Using a solid phase binding assay, we …

Bacteria in nature are exposed to variations in temperature, and are affected by the
availability of nutrients and water and the presence of toxic molecules. Their reactions to …

The DnaK and DnaJ heat shock proteins function as the primary Hsp70 and Hsp40
homologues, respectively, of Escherichia coli. Intensive studies of various Hsp70 and DnaJ …

The heat shock proteins (HSPs) are encoded by genes whose expression is substantially
increased during stress conditions, such as heat shock, alcohol, inhibitors of energy …