 |
PDBsum entry 5nqs
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transcription
|
PDB id
|
|
|
|
5nqs
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structure of thearabidopsistopless corepressor provides insight into the evolution of transcriptional repression.
|
|
|
Authors
|
|
R.Martin-Arevalillo,
M.H.Nanao,
A.Larrieu,
T.Vinos-Poyo,
D.Mast,
C.Galvan-Ampudia,
G.Brunoud,
T.Vernoux,
R.Dumas,
F.Parcy.
|
|
|
Ref.
|
|
Proc Natl Acad Sci U S A, 2017,
114,
8107-8112.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
|
|
|
|
