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GroEL actively stimulates folding of the endogenous substrate protein PepQ

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  • Jeremy Weaver

    (Texas A&M University
    Present address: Division of Molecular and Cellular Biology, NICHD, National Institutes of Health, Bethesda, Maryland 20892, USA)

  • Mengqiu Jiang

    (Texas A&M University
    State Key Laboratory of Biocontrol, School of Life Science, Sun Yat-sen University)

  • Andrew Roth

    (Texas A&M University)

  • Jason Puchalla

    (Princeton University)

  • Junjie Zhang

    (Texas A&M University)

  • Hays S. Rye

    (Texas A&M University)

Abstract

Many essential proteins cannot fold without help from chaperonins, like the GroELS system of Escherichia coli. How chaperonins accelerate protein folding remains controversial. Here we test key predictions of both passive and active models of GroELS-stimulated folding, using the endogenous E. coli metalloprotease PepQ. While GroELS increases the folding rate of PepQ by over 15-fold, we demonstrate that slow spontaneous folding of PepQ is not caused by aggregation. Fluorescence measurements suggest that, when folding inside the GroEL-GroES cavity, PepQ populates conformations not observed during spontaneous folding in free solution. Using cryo-electron microscopy, we show that the GroEL C-termini make physical contact with the PepQ folding intermediate and help retain it deep within the GroEL cavity, resulting in reduced compactness of the PepQ monomer. Our findings strongly support an active model of chaperonin-mediated protein folding, where partial unfolding of misfolded intermediates plays a key role.

Suggested Citation

  • Jeremy Weaver & Mengqiu Jiang & Andrew Roth & Jason Puchalla & Junjie Zhang & Hays S. Rye, 2017. "GroEL actively stimulates folding of the endogenous substrate protein PepQ," Nature Communications, Nature, vol. 8(1), pages 1-15, August.
  • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15934
    DOI: 10.1038/ncomms15934
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    Cited by:

    1. Wei He & Xinming Li & Hongjuan Xue & Yuanyuan Yang & Jun Mencius & Ling Bai & Jiayin Zhang & Jianhe Xu & Bin Wu & Yi Xue & Shu Quan, 2022. "Insights into the client protein release mechanism of the ATP-independent chaperone Spy," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    2. Ritaban Halder & Daniel A. Nissley & Ian Sitarik & Yang Jiang & Yiyun Rao & Quyen V. Vu & Mai Suan Li & Justin Pritchard & Edward P. O’Brien, 2023. "How soluble misfolded proteins bypass chaperones at the molecular level," Nature Communications, Nature, vol. 14(1), pages 1-17, December.

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