Journal
SCIENCE ADVANCES
Volume 3, Issue 6, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.1601217
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Funding
- Outstanding Young Scientist Foundation of CAS
- Youth Innovation Promotion Association of CAS
- Van Andel Research Institute
- Ministry of Science and Technology (China) [2012ZX09301001, 2012CB910403, 2013CB910600, XDB08020303, 2013ZX09507001]
- NSF [91217311]
- NIH [DK071662, GM102545, GM104212, CA181343]
- Michigan Economic Development Corporation
- Michigan Technology Tri-Corridor [085P1000817]
- Office of Science of the U. S. Department of Energy [DE-AC02-06CH11357]
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TOPLESS are tetrameric plant corepressors of the conserved Tup1/Groucho/TLE (transducin-like enhancer of split) family. We show that they interact through their TOPLESS domains (TPDs) with two functionally important ethylene response factor-associated amphiphilic repression (EAR) motifs of the rice strigolactone signaling repressor D53: the universally conserved EAR-3 and the monocot-specific EAR-2. We present the crystal structure of the monocot-specific EAR-2 peptide in complex with the TOPLESS-related protein 2 (TPR2) TPD, in which the EAR-2 motif binds the same TPD groove as jasmonate and auxin signaling repressors but makes additional contacts with a second TPD site to mediate TPD tetramer-tetramer interaction. We validated the functional relevance of the two TPD binding sites in reporter gene assays and in transgenic rice and demonstrate that EAR-2 binding induces TPD oligomerization. Moreover, we demonstrate that the TPD directly binds nucleosomes and the tails of histones H3 and H4. Higher-order assembly of TPD complexes induced by EAR-2 binding markedly stabilizes the nucleosome-TPD interaction. These results establish a new TPD-repressor binding mode that promotes TPD oligomerization and TPD-nucleosome interaction, thus illustrating the initial assembly of a repressor-corepressor-nucleosome complex.
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