Fig. 7: GroEL locally destabilises the NC prior to encapsulation in GroEL:ES2.
From: GroEL/ES chaperonin unfolds then encapsulates a nascent protein on the ribosome
a Deprotection of NC1-510mut upon binding GroEL. Difference in deuterium uptake after 100 s, between GroEL-bound RNC1-510mut and isolated RNC1-510mut. Values are plotted for individual peptides covering the β-gal NC. Positive values indicate more deuteration of a peptide in the GroEL-bound RNC relative to the isolated RNC. The data are also mapped onto a schematic domain diagram of NC1-510mut. Sites with increased deuterium uptake are shaded in red, sites with unchanged deuterium uptake are shaded in grey, and sites on the NC that crosslinked to GroEL are indicated using orange asterisks. Unshaded regions are not covered by peptides. Data are presented as mean ± SD, n = 3 independent labelling reactions. b Conformational dynamics of NC1-510mut compared to native β-gal. Difference in deuterium uptake after 100 s, between isolated RNC1-510mut and native full-length β-gal. Positive values indicate more deuteration of a peptide in the RNC relative to native β-gal. Data are presented as mean ± SD, n = 3 independent labelling reactions. c No deprotection of NC encapsulated by GroEL/ES. As in (a), except isolated RNC1-510mut is compared to the complex with GroEL/ES/ATP/BeFx. Data are presented as mean ± SD, n = 3 independent labelling reactions. Source data are provided in Supplementary Data 1.
