Martin-Arevalillo, R, Nanao, MH, Larrieu, A orcid.org/0000-0002-9024-5348 et al. (7 more authors) (2017) Structure of the Arabidopsis TOPLESS corepressor provides insight into the evolution of transcriptional repression. Proceedings of the National Academy of Sciences, 114 (30). pp. 8107-8112. ISSN 0027-8424
Abstract
Transcriptional repression involves a class of proteins called corepressors that link transcription factors to chromatin remodeling complexes. In plants such as Arabidopsis thaliana, 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 Arabidopsis 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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | Reproduced in accordance with the publisher's self-archiving policy. |
Keywords: | TOPLESS; coreprocessor; auxin signaling; crystal structure; tetramerization |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 21 Sep 2017 11:38 |
Last Modified: | 18 Jul 2019 12:33 |
Status: | Published |
Publisher: | National Academy of Sciences |
Identification Number: | 10.1073/pnas.1703054114 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:121499 |