Publications by authors named "Ramon Peralta-Martinez"
p53 exerts its tumour suppressor activity by modulating hundreds of genes and it can also repress viral replication. Such is the case of human papillomavirus (HPV) through targeting the E2 master regulator, but the biochemical mechanism is not known. We show that the C-terminal DNA binding domain of HPV16 E2 protein (E2C) triggers heterotypic condensation with p53 at a precise 2/1 E2C/p53 stoichiometry at the onset for demixing, yielding large regular spherical droplets that increase in size with E2C concentration.
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- Viruses have developed specialized methods to exploit host cell processes for their replication, utilizing structures called viral factories (VFs) that act as sites for viral gene function.
- Recent research indicates that these VFs exhibit liquid-like qualities due to a phenomenon called liquid-liquid phase separation (LLPS), particularly in negative stranded RNA viruses towards the end of their infectious cycle.
- Understanding the mechanisms behind viral biomolecular condensation opens avenues for new treatments and enhances our knowledge of cellular gene regulation through similar phase separation processes.