Recognition of transcription termination signal by the nuclear polyadenylated RNA-binding (Nab)3 protein

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F11%3A00049398" target="_blank" >RIV/00216224:14740/11:00049398 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1074/jbc.M110.158774" target="_blank" >http://dx.doi.org/10.1074/jbc.M110.158774</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1074/jbc.M110.158774" target="_blank" >10.1074/jbc.M110.158774</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Recognition of transcription termination signal by the nuclear polyadenylated RNA-binding (Nab)3 protein

Popis výsledku v původním jazyce

Non-coding RNA polymerase II transcripts are processed by the poly(A) independent termination pathway that requires the Nrd1 complex. The Nrd1 complex includes two RNA-binding proteins, the nuclear polyadenylated RNA-binding (Nab)3 and the nuclear pre-mRNA down-regulation (Nrd)1 that bind their specific termination elements. Here we report the solution structure of the RNA-recognition motif (RRM) of Nab3 in complex with a UCUU oligonucleotide, representing the Nab3 termination element. The structure shows that the first three nucleotides of UCUU are accommodated on the beta-sheet surface of Nab3 RRM, but reveals a sequence specific recognition only for the central cytidine and uridine. The specific contacts we identified are important for binding affinity in vitro as well as for yeast viability. Further, we show that both RNA-binding motifs of Nab3 and Nrd1 alone bind their termination elements with a weak affinity.

Název v anglickém jazyce

Recognition of transcription termination signal by the nuclear polyadenylated RNA-binding (Nab)3 protein

Popis výsledku anglicky

Non-coding RNA polymerase II transcripts are processed by the poly(A) independent termination pathway that requires the Nrd1 complex. The Nrd1 complex includes two RNA-binding proteins, the nuclear polyadenylated RNA-binding (Nab)3 and the nuclear pre-mRNA down-regulation (Nrd)1 that bind their specific termination elements. Here we report the solution structure of the RNA-recognition motif (RRM) of Nab3 in complex with a UCUU oligonucleotide, representing the Nab3 termination element. The structure shows that the first three nucleotides of UCUU are accommodated on the beta-sheet surface of Nab3 RRM, but reveals a sequence specific recognition only for the central cytidine and uridine. The specific contacts we identified are important for binding affinity in vitro as well as for yeast viability. Further, we show that both RNA-binding motifs of Nab3 and Nrd1 alone bind their termination elements with a weak affinity.

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

The Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

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Svazek periodika

286

Číslo periodika v rámci svazku

5

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

3645-3657

Kód UT WoS článku

000286653200048

EID výsledku v databázi Scopus

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