Chemical shift assignments of the ACID domain of MED25, a subunit of the mediator complex in Arabidopsis thaliana.
Biomol NMR Assign
; 18(1): 27-31, 2024 Jun.
Article
in En
| MEDLINE
| ID: mdl-38334938
ABSTRACT
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 ß-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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Arabidopsis
/
Nuclear Magnetic Resonance, Biomolecular
/
Arabidopsis Proteins
/
Mediator Complex
/
Protein Domains
Language:
En
Journal:
Biomol NMR Assign
Year:
2024
Document type:
Article