Abstract
Chimeric peptides, comprising a DnaK-binding sequence of L-amino acid residues (motif k) and an exclusive DnaJ-binding sequence of D-amino acid residues (motif j) connected through a 22-residue linker, were examined as minisubstrates for the DnaK chaperone system. The DnaJ-stimulated ATPase activity of DnaK was three times higher in the presence of the chimeric peptides p jk or p kj than in the simultaneous presence of the corresponding single-motif peptides ala-p5 ( k motif) plus D-p5 ( j motif). Apparently, p jk and p kj mimic unfolded proteins by forming ternary (ATP·DnaK)·peptide·DnaJ complexes which favor cis-interaction of DnaJ with DnaK. Consistent with this interpretation, the specific stimulatory effect of the chimeric peptides was abolished by either single-motif peptide in excess.
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