A large variety of stress conditions including physicochemical factors induce the synthesis of
more than 20 heat shock proteins (HSPs). In E. coli, the heat shock response to temperature …

Determination of the structure of the substrate binding domain of the Escherichia coli Hsp70
chaperone, DnaK, and the biochemical characterisation of the motif it recognizes within …

Hsp70 chaperones assist protein folding by ATP‐dependent association with linear peptide
segments of a large variety of folding intermediates. The molecular basis for this ability to …

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 70 kDa heat shock proteins (the Hsp70 family) assist refolding of their substrates
through ATP-controlled binding. We have analyzed mutants of DnaK, an Hsp70 homolog …

▪ 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 heat shock response (HSR) is a homeostatic response that maintains the proper protein-
folding environment in the cell. This response is universal, and many of its components are …

The evolutionarily conserved DnaJ proteins are essential components of Hsp70 chaperone
systems. The DnaJ homologue of Escherichia coli associates with chaperone substrates …

Screening of arrays and libraries of compounds is well-established as a high-throughput
method for detecting and analyzing interactions in both biological and chemical systems …

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