Cooperative Subunit Refolding of a Light-Harvesting Protein through a Self-Chaperone Mechanism

Alistair J. Laos, Jacob C. Dean, Zi S.D. Toa, Krystyna E. Wilk, Gregory D. Scholes, Paul M.G. Curmi, Pall Thordarson

Research output: Contribution to journalArticle

4 Scopus citations

Abstract

The fold of a protein is encoded by its amino acid sequence, but how complex multimeric proteins fold and assemble into functional quaternary structures remains unclear. Here we show that two structurally different phycobiliproteins refold and reassemble in a cooperative manner from their unfolded polypeptide subunits, without biological chaperones. Refolding was confirmed by ultrafast broadband transient absorption and two-dimensional electronic spectroscopy to probe internal chromophores as a marker of quaternary structure. Our results demonstrate a cooperative, self-chaperone refolding mechanism, whereby the β-subunits independently refold, thereby templating the folding of the α-subunits, which then chaperone the assembly of the native complex, quantitatively returning all coherences. Our results indicate that subunit self-chaperoning is a robust mechanism for heteromeric protein folding and assembly that could also be applied in self-assembled synthetic hierarchical systems.

Original languageEnglish (US)
Pages (from-to)8384-8388
Number of pages5
JournalAngewandte Chemie - International Edition
Volume56
Issue number29
DOIs
StatePublished - Jan 1 2017

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)

Keywords

  • cooperative effects
  • protein complexes
  • protein folding
  • self-assembly
  • ultrafast spectroscopy

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