Three Stages of Nascent Protein Translocation Through the Ribosome Exit Tunnel
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F24%3A43930038" target="_blank" >RIV/60461373:22340/24:43930038 - isvavai.cz</a>
Výsledek na webu
<a href="https://wires.onlinelibrary.wiley.com/doi/10.1002/wrna.1873" target="_blank" >https://wires.onlinelibrary.wiley.com/doi/10.1002/wrna.1873</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/wrna.1873" target="_blank" >10.1002/wrna.1873</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Three Stages of Nascent Protein Translocation Through the Ribosome Exit Tunnel
Popis výsledku v původním jazyce
All proteins in living organisms are produced in ribosomes that facilitate the translation of genetic information into a sequence of amino acid residues. During translation, the ribosome undergoes initiation, elongation, termination, and recycling. In fact, peptide bonds are formed only during the elongation phase, which comprises periodic association of transfer RNAs and multiple auxiliary proteins with the ribosome and the addition of an amino acid to the nascent polypeptide one at a time. The protein spends a considerable amount of time attached to the ribosome. Here, we conceptually divide this portion of the protein lifetime into three stages. We define each stage on the basis of the position of the N-terminus of the nascent polypeptide within the ribosome exit tunnel and the context of the catalytic center. We argue that nascent polypeptides experience a variety of forces that determine how they translocate through the tunnel and interact with the tunnel walls. We review current knowledge about nascent polypeptide translocation and identify several white spots in our understanding of the birth of proteins.
Název v anglickém jazyce
Three Stages of Nascent Protein Translocation Through the Ribosome Exit Tunnel
Popis výsledku anglicky
All proteins in living organisms are produced in ribosomes that facilitate the translation of genetic information into a sequence of amino acid residues. During translation, the ribosome undergoes initiation, elongation, termination, and recycling. In fact, peptide bonds are formed only during the elongation phase, which comprises periodic association of transfer RNAs and multiple auxiliary proteins with the ribosome and the addition of an amino acid to the nascent polypeptide one at a time. The protein spends a considerable amount of time attached to the ribosome. Here, we conceptually divide this portion of the protein lifetime into three stages. We define each stage on the basis of the position of the N-terminus of the nascent polypeptide within the ribosome exit tunnel and the context of the catalytic center. We argue that nascent polypeptides experience a variety of forces that determine how they translocate through the tunnel and interact with the tunnel walls. We review current knowledge about nascent polypeptide translocation and identify several white spots in our understanding of the birth of proteins.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10610 - Biophysics
Návaznosti výsledku
Projekt
<a href="/cs/project/GA23-05557S" target="_blank" >GA23-05557S: Vstříc atomárnímu pochopení prvních okamžiků života proteinu</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2024
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Wiley Interdisciplinary Reviews-RNA
ISSN
1757-7004
e-ISSN
1757-7012
Svazek periodika
15
Číslo periodika v rámci svazku
6
Stát vydavatele periodika
GB - Spojené království Velké Británie a Severního Irska
Počet stran výsledku
10
Strana od-do
"e1873"
Kód UT WoS článku
001368129500001
EID výsledku v databázi Scopus
2-s2.0-85208491593