5JHP

Crystal structure of the rice Topless related protein 2 (TPR2) N-terminal topless domain (1-209) L179A and I195A mutant in complex with rice D53 repressor EAR peptide motif

Summary for 5JHP

• Entry DOI: 10.2210/pdb5jhp/pdb
• Related: 5J9K 5JA5 5JGC
• Descriptor: Protein TPR1, The rice D53 EAR peptide (794-808) (2 entities in total)
• Functional Keywords: transcription repression, transcriptional corepressor topless, alpha-helical structure, tetramer, transcriptional repressor d53, transcription
• Biological source: Oryza sativa (Rice); More
• Total number of polymer chains: 5
• Total formula weight: 101142.76

Authors

Ke, J.,Ma, H.,Gu, X.,Brunzelle, J.S.,Xu, H.E.,Melcher, K. (deposition date: 2016-04-21, release date: 2017-07-05, Last modification date: 2023-09-27)

Primary citation

Ma, H.,Duan, J.,Ke, J.,He, Y.,Gu, X.,Xu, T.H.,Yu, H.,Wang, Y.,Brunzelle, J.S.,Jiang, Y.,Rothbart, S.B.,Xu, H.E.,Li, J.,Melcher, K.
A D53 repression motif induces oligomerization of TOPLESS corepressors and promotes assembly of a corepressor-nucleosome complex.
Sci Adv, 3:e1601217-e1601217, 2017

PubMed Abstract: 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.

PubMed: 28630893
DOI: 10.1126/sciadv.1601217

Experimental method

X-RAY DIFFRACTION (3.15 Å)