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Solution structure of the N-terminal transactivation domain of ERM modified by SUMO-1.

par Lens, Zoé ;Dewitte, Frédérique;Monte, Didier;Baert, Jean-Luc;Bompard, Coralie;Sénéchal, Magalie;Van Lint, Carine ;De Launoit, Yvan ;Villeret, Vincent ;Verger, Alexis
Référence Biochemical and biophysical research communications, 399, 1, page (104-110)
Publication Publié, 2010

Article révisé par les pairs

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Résumé :

ERM is a member of the PEA3 group of the Ets transcription factor family that plays important roles in development and tumorigenesis. The PEA3s share an N-terminal transactivation domain (TADn) whose activity is inhibited by small ubiquitin-like modifier (SUMO). However, the consequences of sumoylation and its underlying molecular mechanism remain unclear. The domain structure of ERM TADn alone or modified by SUMO-1 was analyzed using small-angle X-ray scattering (SAXS). Low resolution shapes determined ab initio from the scattering data indicated an elongated shape and an unstructured conformation of TADn in solution. Covalent attachment of SUMO-1 does not perturb the structure of TADn as indicated by the linear arrangement of the SUMO moiety with respect to TADn. Thus, ERM belongs to the growing family of proteins that contain intrinsically unstructured regions. The flexible nature of TADn may be instrumental for ERM recognition and binding to diverse molecular partners.