4.6 Article

Structural basis for brassinosteroid response by BIL1/BZR1

Journal

NATURE PLANTS
Volume 4, Issue 10, Pages 771-776

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/s41477-018-0255-1

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Funding

  1. Japan Society for the Promotion of Science (JSPS) [17H05835]
  2. Platform for Drug Discovery, Informatics, and Structural Life Science from the Ministry of Education, Culture, Sports, Science and Technology of Japan (MEXT)
  3. Basis for Supporting Innovative Drug Discovery and Life Science Research from the MEXT
  4. Core Research for Evolutional Science and Technology (CREST) Program of Japan Science and Technology Agency (JST)
  5. Grants-in-Aid for Scientific Research [17H05835] Funding Source: KAKEN

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BRZ-INSENSITIVE-LONG HYPOCOTYL 1 (BIL1)/BRASSINAZOLE-RESISTANT 1 (BZR1) is a master transcription factor of brassinosteroid (BR) signalling. The varieties of nucleobase recognition of the NN-BRRE-core motif (NNCGTG), one of variant G-box motifs, distinguish BIL1/BZR1 from basic helix-loop-helix transcription factors, underlying the specific regulation of BR-responsive genes. Here, we show the non-canonical bHLH dimer formation of BIL1/BZR1 to optimize the interaction network with DNA and the orientation of a key residue for NN-BRRE-core motif recognition.

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