title: Solution structure of the N-terminal transactivation domain of ERM modified by SUMO-1.
abstract: 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.
authors.affiliation: IRI USR CNRS, Parc CNRS de la Haute Borne, Villeneuve d'Ascq, France.
authors.forename: Zoé
authors.initials: Z
authors.lastname: Lens
authors.forename: Frédérique
authors.initials: F
authors.lastname: Dewitte
authors.forename: Didier
authors.initials: D
authors.lastname: Monté
authors.forename: Jean-Luc
authors.initials: JL
authors.lastname: Baert
authors.forename: Coralie
authors.initials: C
authors.lastname: Bompard
authors.forename: Magalie
authors.initials: M
authors.lastname: Sénéchal
authors.forename: Carine
authors.initials: C
authors.lastname: Van Lint
authors.forename: Yvan
authors.initials: Y
authors.lastname: de Launoit
authors.forename: Vincent
authors.initials: V
authors.lastname: Villeret
authors.forename: Alexis
authors.initials: A
authors.lastname: Verger
mesh_terms: D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D017434:Protein Structure, Tertiary; D025842:SUMO-1 Protein / Q000378:metabolism*; D053838:Scattering, Small Angle; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015533:Transcriptional Activation; D014961:X-Ray Diffraction
chemical_list: D004268:DNA-Binding Proteins; C086680:ETV5 protein, human; D025842:SUMO-1 Protein; C495501:SUMO1 protein, human; D014157:Transcription Factors