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Tuning Degradation to Achieve Specific and Efficient Protein Depletion
Published on: July 20, 2019
Active core structure of terfestatin A, a new specific inhibitor of auxin signaling
Ken-ichiro Hayashi1, Atsushi Yamazoe, Yuki Ishibashi
1Department of Biochemistry, Okayama University of Science, 1-1 Ridai-cho, Okayama City 700-0005, Japan. hayashi@dbc.ous.ac.jp
Abstract:
The auxins, plant hormones, regulate many aspects of the growth and development of plants. Terfestatin A (TrfA), a novel auxin signaling inhibitor, was identified in a screen of Streptomyces sp. F40 extracts for inhibition of the expression of an auxin-inducible gene. However, the mode of action of TrfA has not been elucidated. To identify the active core structure, 25 derivatives of TrfA were synthesized and their inhibitory activities against auxin-inducible gene expression were evaluated. The structure-activity relationships revealed the essential active core structure of TrfA, 3-butoxy-4-methylbiphenyl-2,6-diol, which will lead to the design of biotin-tagged active TrfA.
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