4.6 Article

Structure of the SHR-SCR heterodimer bound to the BIRD/IDD transcriptional factor JKD

期刊

NATURE PLANTS
卷 3, 期 3, 页码 -

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NATURE PUBLISHING GROUP
DOI: 10.1038/nplants.2017.10

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资金

  1. MEXT, Japan
  2. Core Research for Evolutionary Science and Technology (CREST)
  3. Japan Science and Technology Agency
  4. National Institutes of Health, United States [R01 GM100051]
  5. Grants-in-Aid for Scientific Research [25440025, 16H06380, 16H06467] Funding Source: KAKEN

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The plant-specific GAI, RGA and SCR (GRAS) family proteins play critical roles in plant development and signalling. Two GRAS proteins, SHORT-ROOT (SHR) and SCARECROW (SCR), cooperatively direct asymmetric cell division and the patterning of root cell types by transcriptional control in conjunction with BIRD/INDETERMINATE DOMAIN (IDD) transcription factors, although precise details of these specific interactions and actions remain unknown. Here, we present the crystal structures of the SHR-SCR binary and JACKDAW (JKD)/IDD10-SHR-SCR ternary complexes. Each GRAS domain comprises one alpha/beta core subdomain with an alpha-helical cap that mediates heterodimerization by forming an intermolecular helix bundle. The alpha/beta core subdomain of SHR forms the BIRD binding groove, which specifically recognizes the zinc fingers of JKD. We identified a conserved SHR-binding motif in 13 BIRD/IDD transcription factors. Our results establish a structural basis for GRAS-GRAS and GRAS-BIRD interactions and provide valuable clues towards our understanding of these regulators, which are involved in plant-specific signalling networks.

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