Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein

Sheila Tuyet Tang, HC Chang, A Roeben, D Wischnewski, N Wischnewski, MJ Kerner, FU Hartl, M Hayer-Hartl

    Research output: Contribution to journalJournal articleResearchpeer-review

    Abstract

    GroEL and GroES form a chaperonin nano-cage for proteins up to similar to 60 kDa to fold in isolation. Here we explored the structural features of the chaperonin cage critical for rapid folding of encapsulated substrates. Modulating the volume of the GroEL central cavity affected folding speed in accordance with confinement theory. Small proteins (similar to 30 kDa) folded more rapidly as the size of the cage was gradually reduced to a point where restriction in space slowed folding dramatically. For larger proteins (similar to 40-50 kDa), either expanding or reducing cage volume decelerated folding. Additionally, interactions with the C-terminal, mildly hydrophobic Gly-Gly-Met repeat sequences of GroEL protruding into the cavity, and repulsion effects from the negatively charged cavity wall were required for rapid folding of some proteins. We suggest that by combining these features, the chaperonin cage provides a physical environment optimized to catalyze the structural annealing of proteins with kinetically complex folding pathways.
    Original languageEnglish
    JournalCell
    Volume125
    Issue number5
    Pages (from-to)903-914
    ISSN0092-8674
    DOIs
    Publication statusPublished - 2006

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