Nature Communications Gao Ning's research group reveals the co-translational folding mechanism of eukaryotic nascent peptide chains

Protein biosynthesis catalyzed by ribosomes is one of the most sophisticated and critical life activities in cells

RAC is a stable heterodimer composed of Hsp40 and Hsp70, which is highly conserved in eukaryotes, and its corresponding proteins in yeast are Zuo1 and Ssz1

On June 14, 2022, Gao Ning's research group from the School of Life Sciences and Life Center of Peking University published a research paper entitled Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding online in Nature Communications

First, structural analysis found that, consistent with the first RAC-ribosome low-resolution structure published by the research group in 2014 [3], the N-terminal and C-terminal domains of Zuo1 spatially bind to the large and small subunits of the ribosome, respectively.

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By local classification and computation for Zuo1-NTD, this study resolved the near-full-length RAC structure for the first time (Fig.

Based on these new structural observations and existing literature reports, this study proposes a schematic diagram of the working mechanism of the RAC-Ssb system (Fig.

Figure 2 Molecular mechanism of the RAC-Ssb co-translational folding system

Professor Gao Ning is the corresponding author of the paper, and Chen Yan (graduated), a 2016 doctoral student in the research group, is the first author of this paper

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