7ET4

Crystal structure of Arabidopsis TEM1 AP2 domain

Summary for 7ET4

• Entry DOI: 10.2210/pdb7et4/pdb
• Descriptor: AP2/ERF and B3 domain-containing transcription repressor TEM1, DNA (12-mer), ... (4 entities in total)
• Functional Keywords: gene regulation, flowering time regulation, plant protein, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Total number of polymer chains: 12
• Total formula weight: 84751.95

Authors

Hu, H.,Du, J. (deposition date: 2021-05-12, release date: 2021-09-15, Last modification date: 2023-11-29)

Primary citation

Hu, H.,Tian, S.,Xie, G.,Liu, R.,Wang, N.,Li, S.,He, Y.,Du, J.
TEM1 combinatorially binds to FLOWERING LOCUS T and recruits a Polycomb factor to repress the floral transition in Arabidopsis.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: TEMPRANILLO 1 (TEM1) is a transcriptional repressor that participates in multiple flowering pathways and negatively regulates the juvenile-to-adult transition and the flowering transition. To understand the molecular basis for the site-specific regulation of () by TEM1, we determined the structures of the two plant-specific DNA-binding domains in TEM1, AP2 and B3, in complex with their target DNA sequences from the gene 5'-untranslated region (5'-UTR), revealing the molecular basis for TEM1 specificity for its DNA targets. In vitro binding assays revealed that the combination of the AP2 and B3 binding sites greatly enhanced the overall binding of TEM1 to the 5'-UTR, indicating TEM1 combinatorically recognizes the gene 5'-UTR. We further showed that TEM1 recruits the Polycomb repressive complex 2 (PRC2) to the 5'-UTR. The simultaneous binding of the TEM1 AP2 and B3 domains to is necessary for deposition of H3K27me3 at the 5'-UTR and for the flowering repressor function of TEM1. Overall, our data suggest that the combinatorial recognition of 5'-UTR by TEM1 ensures H3K27me3 deposition to precisely regulate the floral transition.

PubMed: 34446554
DOI: 10.1073/pnas.2103895118

Experimental method

X-RAY DIFFRACTION (2.7 Å)