Assessment of substrate-stabilizing factors for DnaK on the folding of aggregation-prone proteins

Kisun Ryu, Chul Woo Kim, Byung Hee Kim, Kyoung Sim Han, Kyun Hwan Kim, Seong Il Choi, Baik L. Seong

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

Abstract

Hydrophobic interactions between molecular chaperones and their nonnative substrates have been believed to be mainly responsible for both substrate recognition and stabilization against aggregation. However, the hydrophobic contact area between DnaK and its substrate proteins is very limited and other factors of DnaK for the substrate stabilization could not be excluded. Here, we covalently fused DnaK to the N-termini of aggregation-prone proteins in vivo. In the context of a fusion protein, DnaK has the ability to efficiently solubilize its linked proteins. The point mutation of the residue of DnaK critical for the substrate recognition and the deletion of the C-terminal substrate-binding domain did not have significant effect on the solubilizing ability of DnaK. The results imply that other factors of DnaK, distinct from the hydrophobic shielding of folding intermediates, also contributes to stabilization of its noncovalently bound substrates against aggregation. Elucidation of the nature of these factors would further enhance our understanding of the substrate stabilization of DnaK for expedited protein folding.

Original languageEnglish
Pages (from-to)74-79
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume373
Issue number1
DOIs
Publication statusPublished - 2008 Aug 15

Bibliographical note

Funding Information:
This work was supported in part by the Microbial Genomics R&D Grants from the Ministry of Science and Technology of Korean Government (Grant No. MG05-0306-3-0) and the Korea Research Foundation Grant by the Korean Government (Grant No. KRF-2004-005-C00148).

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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