FEBS Letters | |
cis‐Effect of DnaJ on DnaK in ternary complexes with chimeric DnaK/DnaJ‐binding peptides | |
Christen, Philipp1  Han, Wanjiang1  | |
[1] Biochemisches Institut der Universität Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland | |
关键词: Molecular chaperone; Hsp70; Hsp40; DnaK; DnaJ; Chimeric DnaK/DnaJ-binding peptides; Hsp70; 70-kDa heat shock protein; Hsp40; 40-kDa heat shock protein; acrylodan; 6-acryloyl-2-dimethylaminonaphthalene; a-; acrylodan-labeled; | |
DOI : 10.1016/S0014-5793(04)00290-X | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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 pjk or pkj than in the simultaneous presence of the corresponding single-motif peptides ala-p5 (k motif) plus D-p5 (j motif). Apparently, pjk and pkj 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.
【 授权许可】
Unknown
【 预 览 】
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