TY - JOUR
T1 - Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures
AU - Sastry, M. S.R.
AU - Korotkov, Konstantin
AU - Brodsky, Yan
AU - Baneyx, François
PY - 2002/11/29
Y1 - 2002/11/29
N2 - The Escherichia coli chromosome contains several uncharacterized heat-inducible loci that may encode novel molecular chaperones or proteases. Here we show that the 31-kDa product of the yedU gene is an efficient homodimeric molecular chaperone that is conserved in a number of pathogenic eubacteria and fungi. Heat shock protein (Hsp) 31 relies on temperature-driven conformational changes to expose structured hydrophobic domains that are likely responsible for substrate binding. Complementing the function of refolding, remodeling, and holding chaperones, Hsp 31 preferentially interacts with early unfolding intermediates and rapidly releases them in an active form after transfer to low temperatures. Although Hsp 31 does not appear to exhibit intrinsic ATPase activity, binding of ATP at high temperatures restricts the size or availability of the substrate binding site, thereby modulating chaperone activity. The possible role of ATP in coordinating the function of the cellular complement of molecular chaperones is discussed.
AB - The Escherichia coli chromosome contains several uncharacterized heat-inducible loci that may encode novel molecular chaperones or proteases. Here we show that the 31-kDa product of the yedU gene is an efficient homodimeric molecular chaperone that is conserved in a number of pathogenic eubacteria and fungi. Heat shock protein (Hsp) 31 relies on temperature-driven conformational changes to expose structured hydrophobic domains that are likely responsible for substrate binding. Complementing the function of refolding, remodeling, and holding chaperones, Hsp 31 preferentially interacts with early unfolding intermediates and rapidly releases them in an active form after transfer to low temperatures. Although Hsp 31 does not appear to exhibit intrinsic ATPase activity, binding of ATP at high temperatures restricts the size or availability of the substrate binding site, thereby modulating chaperone activity. The possible role of ATP in coordinating the function of the cellular complement of molecular chaperones is discussed.
UR - http://www.scopus.com/inward/record.url?scp=0037195791&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037195791&partnerID=8YFLogxK
U2 - 10.1074/jbc.M205800200
DO - 10.1074/jbc.M205800200
M3 - Article
C2 - 12235139
AN - SCOPUS:0037195791
SN - 0021-9258
VL - 277
SP - 46026
EP - 46034
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 48
ER -