PMID:12565879
| Citation |
Malki, A, Kern, R, Abdallah, J and Richarme, G (2003) Characterization of the Escherichia coli YedU protein as a molecular chaperone. Biochem. Biophys. Res. Commun. 301:430-6 |
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| Abstract |
We have cloned, purified to homogeneity, and characterized as a molecular chaperone the Escherichia coli YedU protein. The purified protein shows a single band at 31 kDa on SDS-polyacrylamide gels and forms dimers in solution. Like other chaperones, YedU interacts with unfolded and denatured proteins. It promotes the functional folding of citrate synthase and alpha-glucosidase after urea denaturation and prevents the aggregation of citrate synthase under heat shock conditions. YedU forms complexes with the permanently unfolded protein, reduced carboxymethyl alpha-lactalbumin. In contrast to DnaK/Hsp70, ATP does not stimulate YedU-dependent citrate synthase renaturation and does not affect the interaction between YedU and unfolded proteins, and YedU does not display any peptide-stimulated ATPase activity. We conclude that YedU is a novel chaperone which functions independently of an ATP/ADP cycle. |
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| Keywords |
Animals; Citrate (si)-Synthase/chemistry; Citrate (si)-Synthase/metabolism; Cloning, Molecular; Cyclic AMP/chemistry; Cyclic AMP/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/isolation & purification; Escherichia coli Proteins/metabolism; HSP70 Heat-Shock Proteins/metabolism; Hot Temperature; Lactalbumin/chemistry; Lactalbumin/metabolism; Molecular Chaperones/chemistry; Molecular Chaperones/genetics; Molecular Chaperones/isolation & purification; Molecular Chaperones/metabolism; Molecular Weight; Protein Denaturation; Protein Folding; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; alpha-Glucosidases/chemistry; alpha-Glucosidases/metabolism |
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