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PDBsum entry 5nqs
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Transcription
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PDB id
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5nqs
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PDB id:
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| Name: |
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Transcription
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Title:
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Structure of the arabidopsis thaliana topless n-terminal domain
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Structure:
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Protein topless. Chain: a, b. Synonym: wus-interacting protein 1. Engineered: yes
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Source:
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Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Gene: tpl, wsip1, at1g15750, f7h2.9. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: rosetta de3.
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Resolution:
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2.61Å
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R-factor:
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0.203
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R-free:
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0.247
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Authors:
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M.H.Nanao,M.R.Arevalillo,T.Vinos-Poyo,F.Parcy,R.Dumas
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Key ref:
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R.Martin-Arevalillo
et al.
(2017).
Structure of theArabidopsisTOPLESS corepressor provides insight into the evolution of transcriptional repression.
Proc Natl Acad Sci U S A,
114,
8107-8112.
PubMed id:
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Date:
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21-Apr-17
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Release date:
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26-Jul-17
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PROCHECK
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Headers
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References
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Q94AI7
(TPL_ARATH) -
Protein TOPLESS from Arabidopsis thaliana
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Seq:
Struc:
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1131 a.a.
179 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Proc Natl Acad Sci U S A
114:8107-8112
(2017)
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PubMed id:
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Structure of theArabidopsisTOPLESS corepressor provides insight into the evolution of transcriptional repression.
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R.Martin-Arevalillo,
M.H.Nanao,
A.Larrieu,
T.Vinos-Poyo,
D.Mast,
C.Galvan-Ampudia,
G.Brunoud,
T.Vernoux,
R.Dumas,
F.Parcy.
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ABSTRACT
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Transcriptional repression involves a class of proteins called corepressors that
link transcription factors to chromatin remodeling complexes. In plants such
asArabidopsis 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 theArabidopsisTPL 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.
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