| TRIPSIANES, Konstantinos, A. FRIBERG, Ch. BARRANDON, M. BROOKS, H. VAN TILBEURGH, B. SERAPHIN a Michael SATTLER. A Novel Protein-Protein Interaction in the RES (REtention and Splicing) Complex. Journal of Biological Chemistry. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2014, roč. 289, č. 41, s. 28640-28650. ISSN 0021-9258. Dostupné z: https://dx.doi.org/10.1074/jbc.M114.592311. |
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@article{1231760,
author = {Tripsianes, Konstantinos and Friberg, A. and Barrandon, Ch. and Brooks, M. and van Tilbeurgh, H. and Seraphin, B. and Sattler, Michael},
article_location = {Bethesda, USA},
article_number = {41},
doi = {http://dx.doi.org/10.1074/jbc.M114.592311},
keywords = {MESSENGER-RNA RETENTION; RECOGNITION MOTIF; NMR; YEAST; CRYSTALLOGRAPHY; SPLICEOSOME; SYSTEM; DOMAIN; CORE},
language = {eng},
issn = {0021-9258},
journal = {Journal of Biological Chemistry},
title = {A Novel Protein-Protein Interaction in the RES (REtention and Splicing) Complex},
url = {http://www.jbc.org/content/289/41/28640.long},
volume = {289},
year = {2014}
}
TY - JOUR
ID - 1231760
AU - Tripsianes, Konstantinos - Friberg, A. - Barrandon, Ch. - Brooks, M. - van Tilbeurgh, H. - Seraphin, B. - Sattler, Michael
PY - 2014
TI - A Novel Protein-Protein Interaction in the RES (REtention and Splicing) Complex
JF - Journal of Biological Chemistry
VL - 289
IS - 41
SP - 28640-28650
EP - 28640-28650
PB - Amer. Soc. Biochem. Mol. Biol.
SN - 00219258
KW - MESSENGER-RNA RETENTION
KW - RECOGNITION MOTIF
KW - NMR
KW - YEAST
KW - CRYSTALLOGRAPHY
KW - SPLICEOSOME
KW - SYSTEM
KW - DOMAIN
KW - CORE
UR - http://www.jbc.org/content/289/41/28640.long
L2 - http://www.jbc.org/content/289/41/28640.long
N2 - 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.
ER -
TRIPSIANES, Konstantinos, A. FRIBERG, Ch. BARRANDON, M. BROOKS, H. VAN TILBEURGH, B. SERAPHIN a Michael SATTLER. A Novel Protein-Protein Interaction in the RES (REtention and Splicing) Complex. \textit{Journal of Biological Chemistry}. Bethesda, USA: Amer. Soc. Biochem. Mol. Biol., 2014, roč.~289, č.~41, s.~28640-28650. ISSN~0021-9258. Dostupné z: https://dx.doi.org/10.1074/jbc.M114.592311.
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