Molecular architecture of the ribosome-bound Hepatitis C Virus internal ribosomal entry site RNA

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F15%3A00087262" target="_blank" >RIV/00216224:14740/15:00087262 - isvavai.cz</a>

Výsledek na webu

<a href="http://emboj.embopress.org/content/34/24/3042" target="_blank" >http://emboj.embopress.org/content/34/24/3042</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.15252/embj.201592469" target="_blank" >10.15252/embj.201592469</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Molecular architecture of the ribosome-bound Hepatitis C Virus internal ribosomal entry site RNA

Popis výsledku v původním jazyce

Internal ribosomal entry sites (IRESs) are structured cis-acting RNAs that drive an alternative, cap-independent translation initiation pathway. They are used by many viruses to hijack the translational machinery of the host cell. IRESs facilitate translation initiation by recruiting and actively manipulating the eukaryotic ribosome using only a subset of canonical initiation factor and IRES transacting factors. Here we present cryo-EM reconstructions of the ribosome 80S- and 40S-bound Hepatitis C Virus(HCV) IRES. The presence of four subpopulations for the 80S center dot HCV IRES complex reveals dynamic conformational modes of the complex. At a global resolution of 3.9 angstrom for the most stable complex, a derived atomic model reveals a complex fold of the IRES RNA and molecular details of its interaction with the ribosome. The comparison of obtained structures explains how a modular architecture facilitates mRNA loading and tRNA binding to the P-site.

Název v anglickém jazyce

Molecular architecture of the ribosome-bound Hepatitis C Virus internal ribosomal entry site RNA

Popis výsledku anglicky

Internal ribosomal entry sites (IRESs) are structured cis-acting RNAs that drive an alternative, cap-independent translation initiation pathway. They are used by many viruses to hijack the translational machinery of the host cell. IRESs facilitate translation initiation by recruiting and actively manipulating the eukaryotic ribosome using only a subset of canonical initiation factor and IRES transacting factors. Here we present cryo-EM reconstructions of the ribosome 80S- and 40S-bound Hepatitis C Virus(HCV) IRES. The presence of four subpopulations for the 80S center dot HCV IRES complex reveals dynamic conformational modes of the complex. At a global resolution of 3.9 angstrom for the most stable complex, a derived atomic model reveals a complex fold of the IRES RNA and molecular details of its interaction with the ribosome. The comparison of obtained structures explains how a modular architecture facilitates mRNA loading and tRNA binding to the P-site.

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

EMBO Journal

ISSN

0261-4189

e-ISSN

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Svazek periodika

34

Číslo periodika v rámci svazku

24

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

17

Strana od-do

3042-3058

Kód UT WoS článku

000367918000007

EID výsledku v databázi Scopus

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