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Cotranslational activity of the GroEL chaperonin

ABSTRACT: Various proteins in the cell begin to fold during synthesis at the ribosome, many with the assistance of molecular chaperones. While the cotranslational activity of ribosome-associated chaperones and Hsp70 is frequently studied, the role of Hsp60 chaperonins during protein synthesis remains poorly understood. Here, we studied the binding of E. coli chaperonin GroEL to ribosome-nascent chain complexes (RNCs), to understand GroEL activity during nascent chain (NC) synthesis and folding. Using biochemical reconstitution, structural proteomics and electron microscopy we describe the physical architecture of GroEL:RNC and ATP/BeFx-GroEL/ES:RNC complexes. We show that GroEL engages destabilised nascent chains on the inside of its cavity via the apical domains and disordered C-terminal tails. This GroEL:RNC complex can be capped by GroES on the NC-bound ring, with GroEL but not GroEL/ES binding promoting nascent chain destabilisation. Lastly, we observe that GroEL directly competes with Hsp70 for nascent chain binding. Our findings thus show that GroEL is a versatile chaperone which in addition to its well characterised post-translational activity can affect folding of nascent chains undergoing synthesis.

INSTRUMENT(S):

ORGANISM(S): Escherichia Coli

SUBMITTER: Alzbeta Roeselova

LAB HEAD: David Balchin

PROVIDER: PXD054376 | Pride | 2025-10-14

REPOSITORIES: Pride

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	230907_366.xlsx	Xlsx
	230907_366EL.xlsx	Xlsx
	230907_EL.xlsx	Xlsx
	230907_EL.zip	Other
	231202_366.xlsx	Xlsx

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Cotranslational activity of the GroEL chaperonin

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