The heat shock response of Escherichia coli
F Arsène, T Tomoyasu, B Bukau - International journal of food microbiology, 2000 - Elsevier
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 …
more than 20 heat shock proteins (HSPs). In E. coli, the heat shock response to temperature …
Interaction of Hsp70 chaperones with substrates
S Rüdiger, A Buchberger, B Bukau - Nature structural biology, 1997 - nature.com
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 …
chaperone, DnaK, and the biochemical characterisation of the motif it recognizes within …
[HTML][HTML] Substrate specificity of the DnaK chaperone determined by screening cellulose‐bound peptide libraries
S Rüdiger, L Germeroth, J Schneider‐Mergener… - The EMBO …, 1997 - embopress.org
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 …
segments of a large variety of folding intermediates. The molecular basis for this ability to …
Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones
T Laufen, MP Mayer, C Beisel… - Proceedings of the …, 1999 - National Acad Sciences
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 …
lifespan of proteins. Central to these activities is the regulation of Hsp70 by DnaJ …
Multistep mechanism of substrate binding determines chaperone activity of Hsp70
MP Mayer, H Schröder, S Rüdiger, K Paal… - Nature structural …, 2000 - nature.com
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 …
through ATP-controlled binding. We have analyzed mutants of DnaK, an Hsp70 homolog …
The anti-sigma factors
KT Hughes, K Mathee - Annual review of microbiology, 1998 - annualreviews.org
▪ 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 …
antagonist of the sigma transcription factor known as the anti-sigma (anti-σ) factor. The …
Convergence of Molecular, Modeling, and Systems Approaches for an Understanding of the Escherichia coli Heat Shock Response
E Guisbert, T Yura, VA Rhodius… - … and Molecular Biology …, 2008 - Am Soc Microbiol
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 …
folding environment in the cell. This response is universal, and many of its components are …
[HTML][HTML] Its substrate specificity characterizes the DnaJ co‐chaperone as a scanning factor for the DnaK chaperone
S Rüdiger, J Schneider‐Mergener, B Bukau - The EMBO journal, 2001 - embopress.org
The evolutionarily conserved DnaJ proteins are essential components of Hsp70 chaperone
systems. The DnaJ homologue of Escherichia coli associates with chaperone substrates …
systems. The DnaJ homologue of Escherichia coli associates with chaperone substrates …
Studying protein–protein interactions using peptide arrays
C Katz, L Levy-Beladev, S Rotem-Bamberger… - Chemical Society …, 2011 - pubs.rsc.org
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 …
method for detecting and analyzing interactions in both biological and chemical systems …
Mechanics of Hsp70 chaperones enables differential interaction with client proteins
R Schlecht, AH Erbse, B Bukau… - Nature structural & …, 2011 - nature.com
Hsp70 chaperones interact with a wide spectrum of substrates ranging from unfolded to
natively folded and aggregated proteins. Structural evidence suggests that bound substrates …
natively folded and aggregated proteins. Structural evidence suggests that bound substrates …