Chemical shift assignments of the ACID domain of MED25, a subunit of the mediator complex in Arabidopsis thaliana.

Yue Xiong, Jiang Zhu, Rui Hu, Ying Li, Yunhuang Yang, Maili Liu

Biomolecular NMR assignments 2024 Jun

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Mediator complex is a key component that bridges various transcription activators and RNA polymerase during eukaryotic transcription initiation. The Arabidopsis thaliana Med25 (aMed25), a subunit of the Mediator complex, plays important roles in regulating hormone signaling, biotic and abiotic stress responses and plant development by interacting with a variety of transcription factors through its activator-interacting domain (ACID). However, the recognition mechanism of aMed25-ACID for various transcription factors remains unknown. Here, we report the nearly complete 1H, 13C, and 15N backbone and side chain resonance assignments of aMED25-ACID (residues 551-681). TALOS-N analysis revealed that aMED25-ACID structure is comprised of three α-helices and seven β-strands, which lacks the C-terminal α-helix existing in the human MED25-ACID. This study lays a foundation for further research on the structure-function relationship of aMED25-ACID. © 2024. The Author(s), under exclusive licence to Springer Nature B.V.

Citation

Yue Xiong, Jiang Zhu, Rui Hu, Ying Li, Yunhuang Yang, Maili Liu. Chemical shift assignments of the ACID domain of MED25, a subunit of the mediator complex in Arabidopsis thaliana. Biomolecular NMR assignments. 2024 Jun;18(1):27-31