 |
PDBsum entry 2jkd
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Gene regulation
|
PDB id
|
|
|
|
2jkd
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Structure of the yeast pml1 splicing factor and its integration into the res complex.
|
 |
|
Authors
|
 |
M.A.Brooks,
A.Dziembowski,
S.Quevillon-Cheruel,
V.Henriot,
C.Faux,
H.Van tilbeurgh,
B.Séraphin.
|
 |
|
Ref.
|
 |
Nucleic Acids Res, 2009,
37,
129-143.
|
 |
|
PubMed id
|
 |
|
 |
|
|
 |
 |
|
Abstract
|
 |
|
The RES complex was previously identified in yeast as a splicing factor
affecting nuclear pre-mRNA retention. This complex was shown to contain three
subunits, namely Snu17, Bud13 and Pml1, but its mode of action remains
ill-defined. To obtain insights into its function, we have performed a
structural investigation of this factor. Production of a short N-terminal
truncation of residues that are apparently disordered allowed us to determine
the X-ray crystallographic structure of Pml1. This demonstrated that it consists
mainly of a FHA domain, a fold which has been shown to mediate interactions with
phosphothreonine-containing peptides. Using a new sensitive assay based on
alternative splice-site choice, we show, however, that mutation of the putative
phosphothreonine-binding pocket of Pml1 does not affect pre-mRNA splicing. We
have also investigated how Pml1 integrates into the RES complex. Production of
recombinant complexes, combined with serial truncation and mutagenesis of their
subunits, indicated that Pml1 binds to Snu17, which itself contacts Bud13. This
analysis allowed us to demarcate the binding sites involved in the formation of
this assembly. We propose a model of the organization of the RES complex based
on these results, and discuss the functional consequences of this architecture.
|
 |
|
|
|
|
 |