ArticlePlant molecular biology2019
The C-terminal WD40 repeats on the TOPLESS co-repressor function as a protein-protein interaction surface.
Article in Plant molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 48 citations in OpenAlex.
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- Transcriptome-wide Identification of Nine Tandem Repeat Protein Families in Roselle (Tropical life sciences research · 2024Article
- A conserved function of corepressors is to nucleate assembly of the transcriptional preinitiation complex.bioRxiv : the preprint server for biology · 2024Article
- Specific members of the TOPLESS family are susceptibility genes for Fusarium wilt in tomato and Arabidopsis.Plant biotechnology journal · 2024Article
- Canonical and Alternative Auxin Signaling Systems in Mono-, Di-, and Tetraploid Potatoes.International journal of molecular sciences · 2023Article
- Cis-regulatory elements and transcription factors related to auxin signaling in the streptophyte algae Klebsormidium nitens.Scientific reports · 2023Article
- RhizogenicProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Head-to-tail polymerization by VEL proteins underpins cold-induced Polycomb silencing in flowering control.Cell reports · 2022Article
- TOPLESS in the regulation of plant immunity.Plant molecular biology · 2022Review
- Defense response changes in roots of oil palm (Elaeis guineensis Jacq.) seedlings after internal symptoms of Ganoderma boninense Pat. infection.BMC plant biology · 2022Article
- Creativity comes from interactions: modules of protein interactions in plants.The FEBS journal · 2022Review
- Genome-Wide Identification, Characterization and Expression Analysis of the JAZ Gene Family in Resistance to Gray Leaf Spots in Tomato.International journal of molecular sciences · 2021Article
- TEM1 combinatorially binds toProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Repression by theeLife · 2021Article
- Investigation of the role of AcTPR2 in kiwifruit and its response to Botrytis cinerea infection.BMC plant biology · 2020Article
- Evolution of the Auxin Response Factors from charophyte ancestors.PLoS genetics · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
key messageThe two predicted WD40 propellers on TOPLESS function as protein-protein interaction domains. The 1st WD40 propeller mediates interaction with RAV1, and the 2nd WD40 propeller mediates interaction with VRN5. The TOPLESS/TOPLESS-RELATED (TPL/TPR) co-repressor family proteins are known to interact with a wide variety of proteins including transcription factors, Mediator subunits, histone deacetylases, and histone tails. Through these interactions, TPL/TPR act to repress transcription in an increasingly diverse array of plant pathways. Proteins that bind TPL/TPR typically contain one or more Repression Domains (RDs) that mediate the interaction. For example, the well-characterized Ethylene response factor-associated Amphiphilic Repression (EAR) motif is known to facilitate interaction by binding the TOPLESS Domain (TPD) located in the N-terminus. Here we show that in yeast two-hybrid assays, the non-EAR protein, Related to ABI3/VP1-1 (RAV1), binds a novel region located within the first nine WD40-repeats of TPL. Protein modeling and in silico analysis suggest that these nine WD40 repeats may form the first of two WD40 propellers located on C-terminus of TPL. The interaction between RAV1 and the 1st WD40 propeller is conserved with another RAV family member, TEMPRANILLO1 (TEM1) and is mediated by the B3 Repression Domain (BRD) located on both RAV1 and TEM1. Also, the predicted 2nd WD40 propeller was shown in yeast cells to bind Vernalization 5 (VRN5), which contains several unconfirmed partial RDs. Furthermore, we demonstrate that the 1st WD40 propeller of TPL can form a complex with RAV1 both in yeast and in Arabidopsis protoplasts.
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