Cryo-EM optimization and analysis of +1 ribosomal frameshifting
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F24%3A00137938" target="_blank" >RIV/00216224:14740/24:00137938 - isvavai.cz</a>
Result on the web
<a href="https://is.muni.cz/auth/publication/2459121/" target="_blank" >https://is.muni.cz/auth/publication/2459121/</a>
DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Cryo-EM optimization and analysis of +1 ribosomal frameshifting
Original language description
Translation is one of the essential gene regulation machinery that is important for all domains of life. The translation consists of three steps: initiation, elongation and termination, involving a number of translation factors and various types of RNA. During elongation, the anticodon of the transfer RNA (tRNA) is bound to the corresponding codon on the messenger RNA (mRNA), according to the reading frame (RF) of the mRNA, at the ribosomal A site. The correctness of this process can be disrupted during certain conditions, resulting in a shift of the reading frame, also known as frameshifting. We currently know that this phenomenon occurs, but the exact localization of the frameshifting on the ribosome is unknown. Studies have suggested 3 stages of the elongation cycle where this can potentially occur. Here, we focus on the decoding of the mRNA during tRNA accommodation into the A site, with the help of the elongation factor Tu (EF-Tu). To demonstrate whether the shift of the reading frame occurs, we used a biologically derived quadruplet tRNA (qtRNA) that can base-pair with four mRNA bases. We use cryogenic electron microscopy to observe the entire process at near-atomic resolution. Results of the study indicate that there is no frameshift in the reading frame during the decoding of the mRNA by the qtRNA in the A site of the ribosome. méně
Czech name
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Czech description
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Classification
Type
O - Miscellaneous
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/LX22NPO5103" target="_blank" >LX22NPO5103: National Institute of Virology and Bacteriology</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů