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J Biol Chem, Vol. 275, Issue 18, 13755-13758, May 5, 2000
From the Tokyo Institute of Technology, Research Laboratory of
Resources Utilization, R-1, 4259 Nagatsuta, Yokohama 226-8503 and the
Chaperonin GroEL from Escherichia
coli binds to the non-native states of many unrelated proteins,
and GroEL-recognizable structural features have been argued. As model
substrate proteins of GroEL, we used seven artificial proteins
(138~141 residues), each of which has a unique but randomly chosen
amino acid sequence and no propensity to fold into a certain structure.
Two of them were water-soluble, and the rest were soluble in 3 M urea. The soluble ones interacted with GroEL in a manner
similar to that of a natural substrate; they stimulated the ATPase
cycle of GroEL and GroEL/GroES and inhibited GroEL-assisted folding of
other protein. All seven artificial proteins were able to bind to
GroEL. The results suggest that the secondary structure as well as the
specific sequence motif of the substrate proteins are not necessary to
be recognized by GroEL.
GroEL Binds Artificial Proteins with Random Sequences*
, and Department of Biotechnology, Graduate School of
Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan
*
This work was supported by research fellowships from the
Japan Society for the Promotion of Science for Young Scientists.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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