The sulphate-bound form of Pml1 (A, D) is compared with two ligand-bound FHA domains: Rad53:phosphopeptide (10) (B, E) and Ki-67:hNIFK phosphopeptide (29) (C, F). The functional consequences of this architecture.Ī potential phosphopeptide-binding site of Pml1. We propose a model of the organization of the RES complex based on these results, and discuss This analysis allowed us to demarcate the binding sites involved in That Pml1 binds to Snu17, which itself contacts Bud13. Production of recombinant complexes, combined with serial truncation and mutagenesis of their subunits, indicated We have also investigated how Pml1 integrates into Phosphothreonine-binding pocket of Pml1 does not affect pre-mRNA splicing. Using a new sensitive assay based on alternative splice-site choice, we show, however, that mutation of the putative That it consists mainly of a FHA domain, a fold which has been shown to mediate interactions with phosphothreonine-containing Of residues that are apparently disordered allowed us to determine the X-ray crystallographic structure of Pml1. Production of a short N-terminal truncation Into its function, we have performed a structural investigation of this factor. Was shown to contain three subunits, namely Snu17, Bud13 and Pml1, but its mode of action remains ill-defined. The RES complex was previously identified in yeast as a splicing factor affecting nuclear pre-mRNA retention.
0 Comments
Leave a Reply. |