Solution structure of the N-terminal transactivation domain of ERM modified by SUMO-1.
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.
Lens
Zoé
Z
IRI USR CNRS, Parc CNRS de la Haute Borne, Villeneuve d'Ascq, France.
Dewitte
Frédérique
F
Monté
Didier
D
Baert
Jean-Luc
JL
Bompard
Coralie
C
Sénéchal
Magalie
M
Van Lint
Carine
C
de Launoit
Yvan
Y
Villeret
Vincent
V
Verger
Alexis
A
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
D004268:DNA-Binding Proteins; C086680:ETV5 protein, human; D025842:SUMO-1 Protein; C495501:SUMO1 protein, human; D014157:Transcription Factors