Phosphorylation of an intrinsically disordered region of Ets1 shifts a multi-modal interaction ensemble to an auto-inhibitory state

Posted on Posted in AMRC Research

Date: 04 Jan 2018


Multi-modal interactions are frequently observed in intrinsically disordered regions (IDRs) of proteins upon binding to their partners. In many cases, post-translational modifications in IDRs are accompanied by coupled folding and binding. From both molecular simulations and biochemical experiments with mutational studies, we show that the IDR including a Ser rich region (SRR) of the transcription factor Ets1, just before the DNA-binding core domain, undergoes multi-modal interactions when the SRR is not phosphorylated. In the phosphorylated state, the SRR forms a few specific complex structures with the Ets1 core, covering the recognition helix in the core and drastically reducing the DNA binding affinities as the auto-inhibitory state. The binding kinetics of mutated Ets1 indicates that aromatic residues in the SRR can be substituted with other hydrophobic residues for the interactions with the Ets1 core.


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For inquiries regarding this press release

Kazuhiro OGATA

E-mail:   Phone: +81 45 787 2590


Masaaki SHIINA

E-mail:   Phone: +81 45 787 2590


Department of Biochemistry,
Yokohama City University Graduate School of Medicine

Fukuura 3-9, Kanazawa-ku, Yokohama, 236-0004 JAPAN