ArticleProtein science : a publication of the Protein Society2025
The C-terminal tails of GroEL and its mitochondrial and chloroplastic homologs adopt polyproline II helices.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- PolyProline Predictor: A web server for empirical sequence-based prediction of polyproline II helices.Protein science : a publication of the Protein Society · 2026Article
- The C-terminal tails of GroEL and its mitochondrial and chloroplastic homologs adopt polyproline II helices.Protein science : a publication of the Protein Society · 2025Article
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3 authors.
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Abstract
The chaperonin GroEL and its mitochondrial and chloroplastic homologs mHsp60 and Cpn60 are large barrel-like oligomeric proteins. Chaperonins facilitate folding by isolating nascent chains in their hollow interior and undergoing ATP-powered conformational transitions. Due to their vital importance, the structures of GroEL and its homologs were extensively studied by x-ray crystallography and CryoEM, revealing rings containing seven subunits. Each subunit has three folded domains and a 24 residue C-terminal extension. Whereas this C-terminal tail has been reported to bind and stimulate the folding of client proteins, it appears to be blurry or invisible, which suggests disorder. The objective of this study is to characterize conformational preferences in the C-terminal tails of GroEL, mHsp60 and representative Cpn60s using circular dichroism and nuclear magnetic resonance spectroscopies and molecular dynamics simulations. The tails of GroEL and mHsp60 consist of two segments. The first is rich in residues typical of intrinsically disordered proteins (PKNDAADLGA and PKEEKDPGMG in GroEL and mHsp60, respectively) and the second segment consists exclusively (GroEL) or almost entirely (mHsp60) of Gly and Met residues. The spectroscopic results reveal that these C-terminal extensions are not wholly disordered but adopt polyproline II helices whose populations are higher in the second Gly/Met-rich segment. These results are corroborated by MD simulations of GroEL
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