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

Biochemical and Biophysical Research Communications
Zoé LensAlexis Verger

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.

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Citations

May 10, 2011·Annual Review of Biochemistry·Peter C HollenhorstBarbara J Graves
Jun 29, 2011·Protein Expression and Purification·Zoé LensAlexis Verger
Apr 18, 2019·Proceedings of the National Academy of Sciences of the United States of America·Joshua A RibackTobin R Sosnick
Sep 29, 2011·Molecular BioSystems·Pau Bernadó, Dmitri I Svergun
Feb 12, 2020·Journal of Molecular Biology·Patricia L ClarkTobin R Sosnick
Mar 28, 2019·The Journal of Physical Chemistry. B·Upayan BaulD Thirumalai
Nov 23, 2019·Journal of Chemical Theory and Computation·Andrew P Latham, Bin Zhang

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