Amino acids catalyse RNA formation under ambient alkaline conditions
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F25%3A00636642" target="_blank" >RIV/68081707:_____/25:00636642 - isvavai.cz</a>
Výsledek na webu
<a href="https://www.nature.com/articles/s41467-025-60359-3" target="_blank" >https://www.nature.com/articles/s41467-025-60359-3</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41467-025-60359-3" target="_blank" >10.1038/s41467-025-60359-3</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Amino acids catalyse RNA formation under ambient alkaline conditions
Popis výsledku v původním jazyce
RNA and proteins are the foundation of life and a natural starting point to explore its origins. However, the prebiotic relationship between the two is asymmetric. While RNA evolved to assemble proteins from amino acids, a significant mirror-symmetric effect of amino acids to trigger the synthesis of RNA was missing. We describe ambient alkaline conditions where amino acids, without additional chemical activators, promote RNA copolymerisation more than 100-fold, starting from prebiotically plausible ribonucleoside-2 ',3 '-cyclic phosphates. The observed effect is explained by acid-base catalysis, with optimal efficiency at pH values near the amine pKaH. The fold-change in oligomerisation yield is nucleobase-selective, resulting in increased compositional diversity necessary for subsequent molecular evolution and favouring the formation of natural 3 '-5 ' linkages. The elevated pH offers recycling of oligonucleotide sequences back to 2 ',3 '-cyclic phosphates, providing conditions for high-fidelity replication by templated ligation. The findings reveal a clear functional role of amino acids in the evolution of RNA earlier than previously assumed.
Název v anglickém jazyce
Amino acids catalyse RNA formation under ambient alkaline conditions
Popis výsledku anglicky
RNA and proteins are the foundation of life and a natural starting point to explore its origins. However, the prebiotic relationship between the two is asymmetric. While RNA evolved to assemble proteins from amino acids, a significant mirror-symmetric effect of amino acids to trigger the synthesis of RNA was missing. We describe ambient alkaline conditions where amino acids, without additional chemical activators, promote RNA copolymerisation more than 100-fold, starting from prebiotically plausible ribonucleoside-2 ',3 '-cyclic phosphates. The observed effect is explained by acid-base catalysis, with optimal efficiency at pH values near the amine pKaH. The fold-change in oligomerisation yield is nucleobase-selective, resulting in increased compositional diversity necessary for subsequent molecular evolution and favouring the formation of natural 3 '-5 ' linkages. The elevated pH offers recycling of oligonucleotide sequences back to 2 ',3 '-cyclic phosphates, providing conditions for high-fidelity replication by templated ligation. The findings reveal a clear functional role of amino acids in the evolution of RNA earlier than previously assumed.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10608 - Biochemistry and molecular biology
Návaznosti výsledku
Projekt
<a href="/cs/project/GA22-25057S" target="_blank" >GA22-25057S: Studium neenzymatické polymerizace mírně aktivovaných nukleotidových prekurzorů</a><br>
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2025
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Nature Communications
ISSN
2041-1723
e-ISSN
2041-1723
Svazek periodika
16
Číslo periodika v rámci svazku
1
Stát vydavatele periodika
GB - Spojené království Velké Británie a Severního Irska
Počet stran výsledku
9
Strana od-do
5193
Kód UT WoS článku
001503075400015
EID výsledku v databázi Scopus
2-s2.0-105007232051