5NQS

Structure of the Arabidopsis Thaliana TOPLESS N-terminal domain

Summary for 5NQS

• Entry DOI: 10.2210/pdb5nqs/pdb
• Descriptor: Protein TOPLESS (2 entities in total)
• Functional Keywords: topless, transcription factor, plant, auxin, transcription
• Biological source: Arabidopsis thaliana (thale cress)
• Cellular location: Nucleus : Q94AI7
• Total number of polymer chains: 2
• Total formula weight: 50585.63

Authors

Nanao, M.H.,Arevalillo, M.R.,Vinos-Poyo, T.,Parcy, F.,Dumas, R. (deposition date: 2017-04-21, release date: 2017-07-26, Last modification date: 2024-05-01)

Primary citation

Martin-Arevalillo, R.,Nanao, M.H.,Larrieu, A.,Vinos-Poyo, T.,Mast, D.,Galvan-Ampudia, C.,Brunoud, G.,Vernoux, T.,Dumas, R.,Parcy, F.
Structure of the Arabidopsis TOPLESS corepressor provides insight into the evolution of transcriptional repression.
Proc. Natl. Acad. Sci. U.S.A., 114:8107-8112, 2017

PubMed Abstract: Transcriptional repression involves a class of proteins called corepressors that link transcription factors to chromatin remodeling complexes. In plants such as , the most prominent corepressor is TOPLESS (TPL), which plays a key role in hormone signaling and development. Here we present the crystallographic structure of the TPL N-terminal region comprising the LisH and CTLH (C-terminal to LisH) domains and a newly identified third region, which corresponds to a CRA domain. Comparing the structure of TPL with the mammalian TBL1, which shares a similar domain structure and performs a parallel corepressor function, revealed that the plant TPLs have evolved a new tetramerization interface and unique and highly conserved surface for interaction with repressors. Using site-directed mutagenesis, we validated those surfaces in vitro and in vivo and showed that TPL tetramerization and repressor binding are interdependent. Our results illustrate how evolution used a common set of protein domains to create a diversity of corepressors, achieving similar properties with different molecular solutions.

PubMed: 28698367
DOI: 10.1073/pnas.1703054114

Experimental method

X-RAY DIFFRACTION (2.61 Å)