V samotném srdci reiniciace ? eIF3 jako neočekávaný klíčový hráč

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F07%3A00097546" target="_blank" >RIV/61388971:_____/07:00097546 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Association of Eukaryotic Translation Initiation Factor 3 (eIF3) with the 40S Ribosome Post the Terminations Step on Short uORF is a Critical Determinant of its Ability to Reinitiate

Popis výsledku v původním jazyce

Yeast Initiation factor 3 (eIF3) occurs together with the eIF2.GTP.Met-tRNAiMet ternary complex (TC) and eIFs 1 and 5 in a pre-formed unit called the multifactor complex (MFC) that was implicated in playing a critical role in efficient recruitment of TCand mRNA to the 40S ribosomes and stimulation of the post-assembly processes such as scanning and AUG recognition. In a previous study we demonstrated that deletion of the N-terminal domain (NTD) of the TIF32 subunit of eIF3, in the presence of a wild-type gene, completely eliminated association of the mutant MFC with the 40S ribosome without affecting its overall integrity. In addition, we showed that the TIF32-NTD contains a binding site for the C-terminal domain (CTD) of the small ribosomal protein 0A (RPS0A) that is located on the solvent side of the 40S subunit where the main body of eIF3 was proposed to reside

Název v anglickém jazyce

Association of Eukaryotic Translation Initiation Factor 3 (eIF3) with the 40S Ribosome Post the Terminations Step on Short uORF is a Critical Determinant of its Ability to Reinitiate

Popis výsledku anglicky

Yeast Initiation factor 3 (eIF3) occurs together with the eIF2.GTP.Met-tRNAiMet ternary complex (TC) and eIFs 1 and 5 in a pre-formed unit called the multifactor complex (MFC) that was implicated in playing a critical role in efficient recruitment of TCand mRNA to the 40S ribosomes and stimulation of the post-assembly processes such as scanning and AUG recognition. In a previous study we demonstrated that deletion of the N-terminal domain (NTD) of the TIF32 subunit of eIF3, in the presence of a wild-type gene, completely eliminated association of the mutant MFC with the 40S ribosome without affecting its overall integrity. In addition, we showed that the TIF32-NTD contains a binding site for the C-terminal domain (CTD) of the small ribosomal protein 0A (RPS0A) that is located on the solvent side of the 40S subunit where the main body of eIF3 was proposed to reside

Druh

D - Stať ve sborníku

CEP obor

EE - Mikrobiologie, virologie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2007

Kód důvěrnosti údajů

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

Název statě ve sborníku

Annual Conference on Yeasts /35./. Programme. Abstracts

ISBN

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ISSN

1336-4839

e-ISSN

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Počet stran výsledku

1

Strana od-do

23-23

Název nakladatele

SAS

Místo vydání

Bratislava

Místo konání akce

Smolenice

Datum konání akce

16. 5. 2007

Typ akce podle státní příslušnosti

WRD - Celosvětová akce

Kód UT WoS článku

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