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TitleA "spindle and thread" mechanism unblocks p53 translation by modulating N-terminal disorder.
Journal, issue, pagesStructure, Vol. 30, Issue 5, Page 733-742.e7, Year 2022
Publish dateMay 5, 2022
AuthorsMargit Kaldmäe / Thibault Vosselman / Xueying Zhong / Dilraj Lama / Gefei Chen / Mihkel Saluri / Nina Kronqvist / Jia Wei Siau / Aik Seng Ng / Farid J Ghadessy / Pierre Sabatier / Borivoj Vojtesek / Médoune Sarr / Cagla Sahin / Nicklas Österlund / Leopold L Ilag / Venla A Väänänen / Saikiran Sedimbi / Marie Arsenian-Henriksson / Roman A Zubarev / Lennart Nilsson / Philip J B Koeck / Anna Rising / Axel Abelein / Nicolas Fritz / Jan Johansson / David P Lane / Michael Landreh /
PubMed AbstractDisordered proteins pose a major challenge to structural biology. A prominent example is the tumor suppressor p53, whose low expression levels and poor conformational stability hamper the development ...Disordered proteins pose a major challenge to structural biology. A prominent example is the tumor suppressor p53, whose low expression levels and poor conformational stability hamper the development of cancer therapeutics. All these characteristics make it a prime example of "life on the edge of solubility." Here, we investigate whether these features can be modulated by fusing the protein to a highly soluble spider silk domain (NT). The chimeric protein displays highly efficient translation and is fully active in human cancer cells. Biophysical characterization reveals a compact conformation, with the disordered transactivation domain of p53 wrapped around the NT domain. We conclude that interactions with NT help to unblock translation of the proline-rich disordered region of p53. Expression of partially disordered cancer targets is similarly enhanced by NT. In summary, we demonstrate that inducing co-translational folding via a molecular "spindle and thread" mechanism unblocks protein translation in vitro.
External linksStructure / PubMed:35290795
MethodsEM (single particle)
Resolution12.8 Å
Structure data

EMDB-11858:
Recombinant human p53, tetrameric state
Method: EM (single particle) / Resolution: 12.8 Å

Source
  • Homo sapiens (human)

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