 |
PDBsum entry 4x2h
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transcription
|
PDB id
|
|
|
|
4x2h
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural characterization of the chaetomium thermophilum trex-2 complex and its interaction with the mRNA nuclear export factor mex67:mtr2.
|
|
|
Authors
|
|
L.Dimitrova,
E.Valkov,
S.Aibara,
D.Flemming,
S.H.Mclaughlin,
E.Hurt,
M.Stewart.
|
|
|
Ref.
|
|
Structure, 2015,
23,
1246-1257.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The TREX-2 complex integrates mRNA nuclear export into the gene expression
pathway and is based on a Sac3 scaffold to which Thp1, Sem1, Sus1, and Cdc31
bind. TREX-2 also binds the mRNA nuclear export factor, Mex67:Mtr2, through the
Sac3 N-terminal region (Sac3N). Here, we characterize Chaetomium thermophilum
TREX-2, show that the in vitro reconstituted complex has an annular structure,
and define the structural basis for interactions between Sac3, Sus1, Cdc31, and
Mex67:Mtr2. Crystal structures show that the binding of C. thermophilum Sac3N
to the Mex67 NTF2-like domain (Mex67(NTF2L)) is mediated primarily through
phenylalanine residues present in a series of repeating sequence motifs that
resemble those seen in many nucleoporins, and Mlp1 also binds Mex67:Mtr2 using a
similar motif. Deletion of Sac3N generated growth and mRNA export defects in
Saccharomyces cerevisiae, and we propose TREX-2 and Mlp1 function to facilitate
export by concentrating mature messenger ribonucleoparticles at the nuclear pore
entrance.
|
|
|
|
|
|
|
