Three Stages of Nascent Protein Translocation Through the Ribosome Exit Tunnel
The result's identifiers
Result code in 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>
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Three Stages of Nascent Protein Translocation Through the Ribosome Exit Tunnel
Original language description
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.
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
10610 - Biophysics
Result continuities
Project
<a href="/en/project/GA23-05557S" target="_blank" >GA23-05557S: Towards atomistic understanding of the first moments in the life of protein</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
Data specific for result type
Name of the periodical
Wiley Interdisciplinary Reviews-RNA
ISSN
1757-7004
e-ISSN
1757-7012
Volume of the periodical
15
Issue of the periodical within the volume
6
Country of publishing house
GB - UNITED KINGDOM
Number of pages
10
Pages from-to
"e1873"
UT code for WoS article
001368129500001
EID of the result in the Scopus database
2-s2.0-85208491593