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Title: Cooperative Subunit Refolding of a Light‐Harvesting Protein through a Self‐Chaperone Mechanism

Abstract

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.

Authors:
 [1];  [2];  [2];  [3];  [2];  [3]; ORCiD logo [4]
+ Show Author Affiliations
  1. School of Chemistry the Australian Centre for NanoMedicine and the ARC Centre of Excellence in Convergent Bio-Nano Science and Technology The University of New South Wales Sydney 2052 NSW Australia, School of Physics The University of New South Wales Sydney 2052 NSW Australia
  2. Department of Chemistry Princeton University Princeton NJ 08544 USA
  3. School of Physics The University of New South Wales Sydney 2052 NSW Australia
  4. School of Chemistry the Australian Centre for NanoMedicine and the ARC Centre of Excellence in Convergent Bio-Nano Science and Technology The University of New South Wales Sydney 2052 NSW Australia
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1400819
Resource Type:
Publisher's Accepted Manuscript
Journal Name:
Angewandte Chemie
Additional Journal Information:
Journal Name: Angewandte Chemie Journal Volume: 129 Journal Issue: 29; Journal ID: ISSN 0044-8249
Publisher:
Wiley Blackwell (John Wiley & Sons)
Country of Publication:
Germany
Language:
English

Citation Formats

Laos, Alistair J., Dean, Jacob C., Toa, Zi S. D., Wilk, Krystyna E., Scholes, Gregory D., Curmi, Paul M. G., and Thordarson, Pall. Cooperative Subunit Refolding of a Light‐Harvesting Protein through a Self‐Chaperone Mechanism. Germany: N. p., 2017. Web. doi:10.1002/ange.201607921.
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Laos, Alistair J., Dean, Jacob C., Toa, Zi S. D., Wilk, Krystyna E., Scholes, Gregory D., Curmi, Paul M. G., & Thordarson, Pall. Cooperative Subunit Refolding of a Light‐Harvesting Protein through a Self‐Chaperone Mechanism. Germany. https://doi.org/10.1002/ange.201607921
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Laos, Alistair J., Dean, Jacob C., Toa, Zi S. D., Wilk, Krystyna E., Scholes, Gregory D., Curmi, Paul M. G., and Thordarson, Pall. Thu . "Cooperative Subunit Refolding of a Light‐Harvesting Protein through a Self‐Chaperone Mechanism". Germany. https://doi.org/10.1002/ange.201607921.
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@article{osti_1400819,
title = {Cooperative Subunit Refolding of a Light‐Harvesting Protein through a Self‐Chaperone Mechanism},
author = {Laos, Alistair J. and Dean, Jacob C. and Toa, Zi S. D. and Wilk, Krystyna E. and Scholes, Gregory D. and Curmi, Paul M. G. and Thordarson, Pall},
abstractNote = {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.},
doi = {10.1002/ange.201607921},
journal = {Angewandte Chemie},
number = 29,
volume = 129,
place = {Germany},
year = {Thu Feb 09 00:00:00 EST 2017},
month = {Thu Feb 09 00:00:00 EST 2017}
}
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Journal Article:
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Accepted Manuscript (Publisher)
Publisher's Version of Record
https://doi.org/10.1002/ange.201607921
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