1H, 15N and 13C assignments of the N-terminal domain of the Mediator complex subunit MED26
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MED26 is a subunit of the Mediator, a very large complex involved in regulation of gene transcription by RNA Polymerase II. MED26 regulates the switch between initiation and elongation phases of the transcription. This function requires interaction of its N-terminal domain (NTD) with several protein partners implicated in transcriptional regulation. Molecular details of the structure and interaction mode of MED26 NTD would improve understanding of this complex regulation. As a first step towards structural characterization, sequence specific 1H, 13C and 15N assignments for MED26 NTD was performed based on Nuclear Magnetic Resonance spectroscopy. TALOS+ analysis of the chemical shifts data revealed a domain solely composed of helices. Assignments will be further used to solve NMR structure and dynamics of MED26 NTD and investigate the molecular details of its interaction with protein partners.
KeywordsMediator complex Transcriptional regulation Protein–protein interaction NMR resonance assignment
We thank Prof. Joan and Ronald Conaway for the gift of human F-MED26 (Addgene plasmid # 15367). The NMR facilities were funded by the Nord-Pas-de-Calais Regional Council, CNRS, Pasteur Institute of Lille, European Community (FEDER), French Research Ministry and the University of Sciences and Technologies of Lille I. We acknowledge support from TGE RMN THC (FR-3050), ‘Projets Emergents’ Nord-Pas-de-Calais Regional Council and FRABio (FR-3688). R.P. was funded by a fellowship from Nord-Pas-de-Calais Regional Council.
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