A Novel Protein-Protein Interaction in the RES (REtention and Splicing) Complex
作者： Konstantinos Tripsianes , Anders Friberg , Charlotte Barrandon , Mark Brooks , Herman van Tilbeurgh
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摘要: The retention and splicing (RES) complex is a conserved spliceosome-associated module that was shown to enhance of subset transcripts promote the nuclear unspliced pre-mRNAs in yeast. heterotrimeric RES organized around Snu17p protein binds both Bud13p Pml1p subunits. exhibits an RRM domain resembles U2AF homology motif (UHM) harbors Trp residue reminiscent UHM-ligand (ULM). It has therefore been proposed interaction between canonical UHM-ULM complexes. Here, we have used biochemical NMR structural analysis characterize structure yeast Snu17p-Bud13p complex. Unlike known UHMs sequester ULM ligand hydrophobic pocket, utilize large surface formed two helices domain. In total 18 residues wrap helical U-turn-like arrangement. invariant Trp232 located center turn, contacts Snu17p. data are supported by mutational indicate provides extended binding with notably distinct from interactions. Our highlight diversity RRM-protein interactions, analogous one seen for nucleic acid
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