Detailed Information on Publication Record
2014
A Novel Protein-Protein Interaction in the RES (REtention and Splicing) Complex
TRIPSIANES, Konstantinos, A. FRIBERG, Ch. BARRANDON, M. BROOKS, H. VAN TILBEURGH et. al.Basic information
Original name
A Novel Protein-Protein Interaction in the RES (REtention and Splicing) Complex
Authors
TRIPSIANES, Konstantinos (300 Greece, guarantor, belonging to the institution), A. FRIBERG (276 Germany), Ch. BARRANDON (250 France), M. BROOKS (250 France), H. VAN TILBEURGH (250 France), B. SERAPHIN (250 France) and Michael SATTLER (276 Germany)
Edition
Journal of Biological Chemistry, Bethesda, USA, Amer. Soc. Biochem. Mol. Biol. 2014, 0021-9258
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 4.573
RIV identification code
RIV/00216224:14740/14:00079761
Organization unit
Central European Institute of Technology
UT WoS
000343765400052
Keywords in English
MESSENGER-RNA RETENTION; RECOGNITION MOTIF; NMR; YEAST; CRYSTALLOGRAPHY; SPLICEOSOME; SYSTEM; DOMAIN; CORE
Tags
Tags
International impact, Reviewed
Změněno: 25/3/2015 10:06, Martina Prášilová
Abstract
V originále
The retention and splicing (RES) complex is a conserved spliceosome-associated module that was shown to enhance splicing of a subset of transcripts and promote the nuclear retention of unspliced pre-mRNAs in yeast. The heterotrimeric RES complex is organized around the Snu17p protein that binds to both the Bud13p and Pml1p subunits. Snu17p exhibits an RRM domain that resembles a U2AF homology motif (UHM) and Bud13p harbors a Trp residue reminiscent of an UHM-ligand motif (ULM). It has therefore been proposed that the interaction between Snu17p and Bud13p resembles canonical UHM-ULM complexes. Here, we have used biochemical and NMR structural analysis to characterize the structure of the yeast Snu17p-Bud13p complex. Unlike known UHMs that sequester the Trp residue of the ULM ligand in a hydrophobic pocket, Snu17p and Bud13p utilize a large interaction surface formed around the two helices of the Snu17p domain. In total 18 residues of the Bud13p ligand wrap around the Snu17p helical surface in an U-turn-like arrangement. The invariant Trp232 in Bud13p is located in the center of the turn, and contacts surface residues of Snu17p. The structural data are supported by mutational analysis and indicate that Snu17p provides an extended binding surface with Bud13p that is notably distinct from canonical UHM-ULM interactions. Our data highlight structural diversity in RRM-protein interactions, analogous to the one seen for nucleic acid interactions.
Links
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