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.