An essential cellular machinery that has been identified and studied only relatively recently
is a collective of specialized proteins, molecular chaperones, that bind nonnative states of …

▪ 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 …

Hsp70 chaperones assist a large variety of protein folding processes within the entire
lifespan of proteins. Central to these activities is the regulation of Hsp70 by DnaJ …

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 …

Hsp70 chaperones interact with a wide spectrum of substrates ranging from unfolded to
natively folded and aggregated proteins. Structural evidence suggests that bound substrates …

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 …

The chaperone system formed by DnaK, DnaJ and GrpE mediates stress‐dependent
negative modulation of the Escherichia coli heat shock response, probably through …

Hsp70s and J-proteins, which constitute one of the most ubiquitous types of molecular
chaperone machineries, function in a wide variety of cellular processes. J-proteins play a …

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 …