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Newly translated protein misfolding after heat shock and translation during heat shock

ABSTRACT: Correct and efficient folding of nascent proteins to their native state requires support from the protein homeostasis network. We set to examine which newly translated proteins are less thermostable to infer which polypeptides require more time to fold. More specifically, we sought to determine which newly translated proteins are more susceptible to misfolding and aggregation under heat stress using pulse SILAC. These proteins were abundant, shorter, and highly ordered, with a potentially larger hydrophobic core as suggested by their higher hydrophobicity. Notably these proteins contain more β-sheets that typically require more time for folding and were enriched for Hsp70/Ssb and TRiC/CCT binding motifs, suggesting a higher demand for chaperone-assisted folding. These polypeptides were also more often components of stable protein complexes. All evidence combined suggests that a specific subset of newly translated proteins requires more time following synthesis to reach a thermostable native state in the cell.

INSTRUMENT(S): impact II

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Mang Zhu

LAB HEAD: Thibault Mayor

PROVIDER: PXD024336 | Pride | 2022-08-10

REPOSITORIES: Pride

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