Bound substrate polypeptides can generally stabilize the tetradecameric structure of Cpn60 and induce its reassembly from monomers

Jose A. Mendoza, Paul M. Horowitz

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

We demonstrate that the previously observed stabilizing effect by the enzyme rhodanese of the oligomeric structure of Cpn60 is general and can be provided by six other proteins that can interact with Cpn60. All these substrate proteins, which include examples that are monomeric, as well as oligomeric polypeptides in their native states, were shown previously to be assisted in their refolding by the chaperonin. Strikingly, during the disassembly of Cpn60 in the presence of any of the substrate proteins, significant amounts of intermediates were detected. Furthermore, unfolded substrate proteins induce the reassembly of tetradecameric Cpn60 from monomers, and binding of each substrate protein stabilizes Cpn60 quaternary structure.

Original languageEnglish (US)
Pages (from-to)25963-25965
Number of pages3
JournalJournal of Biological Chemistry
Volume269
Issue number42
StatePublished - Oct 21 1994
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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