Transcription-translation coupling at the stages of translation initiation and elongation
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F21%3A00122987" target="_blank" >RIV/00216224:14740/21:00122987 - isvavai.cz</a>
Výsledek na webu
<a href="https://csbmb2021.cz/" target="_blank" >https://csbmb2021.cz/</a>
DOI - Digital Object Identifier
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Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Transcription-translation coupling at the stages of translation initiation and elongation
Popis výsledku v původním jazyce
In Bacteria and Archaea, mRNAs are translated by ribosomes simultaneously as they are transcribed. Visualization of actively transcribing RNA polymerase (RNAP) in E.coli by electron microscopy provided clear insight into physically coupled transcription and translation (CTT) mechanism. Additionally, some biochemical studies confirmed the synchronous rates of transcription and translation in E.coli suggesting a regulation function of the leading ribosome on the RNAP propagation which is crucial for optimal gene expression and genome stability. Here, we present cryo-electron microscopy (cryo-EM) structure of E. coli RNAP core bound to the small ribosomal 30S subunit. Alignment of the RNA exit tunnel of RNAP with the Shine-Dalgarno (SD) binding site of 30S subunit suggests a possible loading mechanism of the mRNA onto the 30S subunit at the stage of translation initiation. The recent expressome structures showed RNAP near the mRNA entry tunnel of the trailing ribosome. This region is more than 80 Å away from the binding site observed in 30S-RNAP structure, suggesting a large-scale relocation of RNAP. The 30S-RNAP and expressome structures may therefore represent interactions that occur at different steps of translation, especially during initiation and elongation. Future studies are aimed at investigating the initiation and elongation steps of CTT using time-resolved cryo-EM approach.
Název v anglickém jazyce
Transcription-translation coupling at the stages of translation initiation and elongation
Popis výsledku anglicky
In Bacteria and Archaea, mRNAs are translated by ribosomes simultaneously as they are transcribed. Visualization of actively transcribing RNA polymerase (RNAP) in E.coli by electron microscopy provided clear insight into physically coupled transcription and translation (CTT) mechanism. Additionally, some biochemical studies confirmed the synchronous rates of transcription and translation in E.coli suggesting a regulation function of the leading ribosome on the RNAP propagation which is crucial for optimal gene expression and genome stability. Here, we present cryo-electron microscopy (cryo-EM) structure of E. coli RNAP core bound to the small ribosomal 30S subunit. Alignment of the RNA exit tunnel of RNAP with the Shine-Dalgarno (SD) binding site of 30S subunit suggests a possible loading mechanism of the mRNA onto the 30S subunit at the stage of translation initiation. The recent expressome structures showed RNAP near the mRNA entry tunnel of the trailing ribosome. This region is more than 80 Å away from the binding site observed in 30S-RNAP structure, suggesting a large-scale relocation of RNAP. The 30S-RNAP and expressome structures may therefore represent interactions that occur at different steps of translation, especially during initiation and elongation. Future studies are aimed at investigating the initiation and elongation steps of CTT using time-resolved cryo-EM approach.
Klasifikace
Druh
O - Ostatní výsledky
CEP obor
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OECD FORD obor
10608 - Biochemistry and molecular biology
Návaznosti výsledku
Projekt
<a href="/cs/project/LL2008" target="_blank" >LL2008: Komunikace mezi transkripcí a translací</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2021
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů