uS3/Rps3 controls fidelity of translation termination and programmed stop codon readthrough in co-operation with eIF3
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F19%3A00519732" target="_blank" >RIV/61388971:_____/19:00519732 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/19:10405277
Result on the web
<a href="https://academic.oup.com/nar/article/47/21/11326/5603221" target="_blank" >https://academic.oup.com/nar/article/47/21/11326/5603221</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/nar/gkz929" target="_blank" >10.1093/nar/gkz929</a>
Alternative languages
Result language
angličtina
Original language name
uS3/Rps3 controls fidelity of translation termination and programmed stop codon readthrough in co-operation with eIF3
Original language description
Ribosome was long considered as a critical yet passive player in protein synthesis. Only recently the role of its basic components, ribosomal RNAs and proteins, in translational control has begun to emerge. Here we examined function of the small ribosomal protein uS3/Rps3, earlier shown to interact with eukaryotic translation initiation factor eIF3, in termination. We identified two residues in consecutive helices occurring in the mRNA entry pore, whose mutations to the opposite charge either reduced (K108E) or increased (R116D) stop codon readthrough. Whereas the latter increased overall levels of eIF3-containing terminating ribosomes in heavy polysomes in vivo indicating slower termination rates, the former specifically reduced eIF3 amounts in termination complexes. Combining these two mutations with the readthrough-reducing mutations at the extreme C-terminus of the a/Tif32 subunit of eIF3 either suppressed (R116D) or exacerbated (K108E) the readthrough phenotypes, and partially corrected or exacerbated the defects in the composition of termination complexes. In addition, we found that K108 affects efficiency of termination in the termination context-specific manner by promoting incorporation of readthrough-inducing tRNAs. Together with the multiple binding sites that we identified between these two proteins, we suggest that Rps3 and eIF3 closely co-operate to control translation termination and stop codon readthrough.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology
Result continuities
Project
<a href="/en/project/GA18-02014S" target="_blank" >GA18-02014S: Neglected players in human non-sense readthrough coming to light.</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nucleic Acids Research
ISSN
0305-1048
e-ISSN
—
Volume of the periodical
47
Issue of the periodical within the volume
21
Country of publishing house
GB - UNITED KINGDOM
Number of pages
18
Pages from-to
11326-11343
UT code for WoS article
000501735200034
EID of the result in the Scopus database
2-s2.0-85075812537