Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F20%3A00114622" target="_blank" >RIV/00216224:14740/20:00114622 - isvavai.cz</a>

Výsledek na webu

<a href="https://watermark.silverchair.com/gkz1163.pdf?token=AQECAHi208BE49Ooan9kkhW_Ercy7Dm3ZL_9Cf3qfKAc485ysgAAArMwggKvBgkqhkiG9w0BBwagggKgMIICnAIBADCCApUGCSqGSIb3DQEHATAeBglghkgBZQMEAS4wEQQM93m65EaHAul9lvZ3AgEQgIICZgl4kN1MOxCY84aEvwwQEi6vjxrtsNYzBuhYRTUjwbqxdd" target="_blank" >https://watermark.silverchair.com/gkz1163.pdf?token=AQECAHi208BE49Ooan9kkhW_Ercy7Dm3ZL_9Cf3qfKAc485ysgAAArMwggKvBgkqhkiG9w0BBwagggKgMIICnAIBADCCApUGCSqGSIb3DQEHATAeBglghkgBZQMEAS4wEQQM93m65EaHAul9lvZ3AgEQgIICZgl4kN1MOxCY84aEvwwQEi6vjxrtsNYzBuhYRTUjwbqxdd</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/nar/gkz1163" target="_blank" >10.1093/nar/gkz1163</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition

Popis výsledku v původním jazyce

Staufen1 (STAU1) is a dsRNA binding protein mediating mRNA transport and localization, translational control and STAU1-mediated mRNA decay (SMD). The STAU1 binding site (SBS) within human ADP-ribosylation factorl (ARF1) 3'UTR binds STAU1 and this downregulates ARF1 cytoplasmic mRNA levels by SMD. However, how STAU1 recognizes specific mRNA targets is still under debate. Our structure of the ARF1 SBS-STAU1 complex uncovers target recognition by STAU1. STAU1 dsRNA binding domain (dsRBD) 4 interacts with two pyrimidines and one purine from the minor groove side via helix alpha 1, the beta 1-beta 2 loop anchors the dsRBD at the end of the dsRNA and lysines in helix alpha 2 bind to the phosphodiester backbone from the major groove side. STAU1 dsRBD3 displays the same binding mode with specific recognition of one guanine base. Mutants disrupting minor groove recognition of ARF1 SBS affect in vitro binding and reduce SMD in vivo. Our data thus reveal how STAU1 recognizes minor groove features in dsRNA relevant for target selection.

Název v anglickém jazyce

Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition

Popis výsledku anglicky

Staufen1 (STAU1) is a dsRNA binding protein mediating mRNA transport and localization, translational control and STAU1-mediated mRNA decay (SMD). The STAU1 binding site (SBS) within human ADP-ribosylation factorl (ARF1) 3'UTR binds STAU1 and this downregulates ARF1 cytoplasmic mRNA levels by SMD. However, how STAU1 recognizes specific mRNA targets is still under debate. Our structure of the ARF1 SBS-STAU1 complex uncovers target recognition by STAU1. STAU1 dsRNA binding domain (dsRBD) 4 interacts with two pyrimidines and one purine from the minor groove side via helix alpha 1, the beta 1-beta 2 loop anchors the dsRBD at the end of the dsRNA and lysines in helix alpha 2 bind to the phosphodiester backbone from the major groove side. STAU1 dsRBD3 displays the same binding mode with specific recognition of one guanine base. Mutants disrupting minor groove recognition of ARF1 SBS affect in vitro binding and reduce SMD in vivo. Our data thus reveal how STAU1 recognizes minor groove features in dsRNA relevant for target selection.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

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)

Rok uplatnění

2020

Kód důvěrnosti údajů

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

Název periodika

Nucleic acids research

ISSN

0305-1048

e-ISSN

—

Svazek periodika

48

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

16

Strana od-do

2091-2106

Kód UT WoS článku

000525957000038

EID výsledku v databázi Scopus

2-s2.0-85081112304