A Novel Protein-Protein Interaction in the RES (REtention and Splicing) Complex

Kód výsledku v IS VaVaI

RIV/00216224:14740/14:00079761 - isvavai.cz

Výsledek na webu

http://www.jbc.org/content/289/41/28640.long

DOI - Digital Object Identifier

10.1074/jbc.M114.592311

Jazyk výsledku

angličtina

Název v původním jazyce

A Novel Protein-Protein Interaction in the RES (REtention and Splicing) Complex

Popis výsledku v původním jazyce

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 theTrp 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.

Název v anglickém jazyce

A Novel Protein-Protein Interaction in the RES (REtention and Splicing) Complex

Popis výsledku anglicky

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 theTrp 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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

EE2.3.20.0042: Internacionalizace programu Strukturní biologie s důrazem na rozvoj nových směrů výzkumu

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2014

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

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Svazek periodika

289

Číslo periodika v rámci svazku

41

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

28640-28650

Kód UT WoS článku

000343765400052

EID výsledku v databázi Scopus

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