Small Ribosomal Protein RPS0 Stimulates Translation Initiation by Mediating 40S-Binding of eIF3 via Its Direct Contact with the eIF3a/TIF32 Subunit

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F12%3A00381937" target="_blank" >RIV/61388971:_____/12:00381937 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1371/journal.pone.0040464" target="_blank" >http://dx.doi.org/10.1371/journal.pone.0040464</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1371/journal.pone.0040464" target="_blank" >10.1371/journal.pone.0040464</a>

Result language

angličtina

Original language name

Small Ribosomal Protein RPS0 Stimulates Translation Initiation by Mediating 40S-Binding of eIF3 via Its Direct Contact with the eIF3a/TIF32 Subunit

Original language description

The ribosome translates information encoded by mRNAs into proteins in all living cells. In eukaryotes, its small subunit together with a number of eukaryotic initiation factors (eIFs) is responsible for locating the mRNA's translational start to properlydecode the genetic message that it carries. This multistep process requires timely and spatially coordinated placement of eIFs on the ribosomal surface. In our long-standing pursuit to map the 40S-binding site of one of the functionally most complex eIFs, yeast multisubunit eIF3, we identified several interactions that placed its major body to the head, beak and shoulder regions of the solvent-exposed side of the 40S subunit. Among them is the interaction between the N-terminal domain (NTD) of the a/TIF32 subunit of eIF3 and the small ribosomal protein RPS0A, residing near the mRNA exit channel

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EE - Microbiology, virology

OECD FORD branch

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Project

<a href="/en/project/GAP305%2F11%2F0172" target="_blank" >GAP305/11/0172: Molecular basis of the gene-specific translational control mechanism of yeast GCN4 and its mammalian functional homologue ATF4.</a><br>

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2012

Confidentiality

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

Name of the periodical

PLoS ONE

ISSN

1932-6203

e-ISSN

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Volume of the periodical

7

Issue of the periodical within the volume

7

Country of publishing house

US - UNITED STATES

Number of pages

9

Pages from-to

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UT code for WoS article

000306436300068

EID of the result in the Scopus database

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