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Cytochrome c prompts the recruitment of its nuclear partners SET/TAF-Iβ and NPM1 into biomolecular condensates

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Casado-Combreras, Miguel Á. | Velázquez-Campoy, Adrián | Martinho, Marlène | Belle, Valérie | de la Rosa, Miguel, A | Díaz-Moreno, Irene

Edité par CCSD ; Elsevier -

International audience. Compartmentalization of proteins by liquid-liquid phase separation (LLPS) is used bycells to control biochemical reactions spatially and temporally. Among them, therecruitment of proteins to DNA foci and nucleolar trafficking occurs by biomolecularcondensation. Within this frame, the oncoprotein SET/TAF-I plays a key role in bothchromatin remodeling and DNA damage response, as does nucleophosmin (NPM1)which indeed participates in nucleolar ribosome synthesis. Whereas phase separationby NPM1 is widely characterized, little is known about that undergone by SET/TAF-I.Here, we show that SET/TAF-I experiences phase transition together with respiratorycytochrome c (Cc), which translocates to the nucleus upon DNA damage. Here wereport the molecular mechanisms governing Cc-induced phase separation of SET/TAF-I and NPM1, where two lysine-rich clusters of Cc are essential to recognize molecularsurfaces on both partners in a specific and coordinated manner. Cc thus emerges as asmall, globular protein with sequence-encoded heterotypic phase-separationproperties.

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