2024
The interplay between peptides and RNA is critical for protoribosome compartmentalization and stability
CODISPOTI, Simone; Tomoko YAMAGUCHI; Mikhail MAKAROV; Valerio G GIACOBELLI; Martin MASEK et al.Základní údaje
Originální název
The interplay between peptides and RNA is critical for protoribosome compartmentalization and stability
Autoři
CODISPOTI, Simone; Tomoko YAMAGUCHI; Mikhail MAKAROV; Valerio G GIACOBELLI; Martin MASEK; Michal H KOLAR; Alma Carolina Sanchez ROCHA; Kosuke FUJISHIMA; Giuliano ZANCHETTA a Klara HLOUCHOVA
Vydání
Nucleic acids research, Oxford, Oxford University Press, 2024, 0305-1048
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10608 Biochemistry and molecular biology
Stát vydavatele
Velká Británie a Severní Irsko
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 13.100
Označené pro přenos do RIV
Ano
Kód RIV
RIV/00216224:90127/24:00139179
Organizační jednotka
CIISB II
UT WoS
EID Scopus
Klíčová slova anglicky
ORIGIN; PARAMETERS; PROTEINS; ACIDS; MODEL
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 26. 3. 2025 23:38, Mgr. Eva Dubská
Anotace
V originále
The ribosome, owing to its exceptional conservation, harbours a remarkable molecular fossil known as the protoribosome. It surrounds the peptidyl transferase center (PTC), responsible for peptide bond formation. While previous studies have demonstrated the PTC activity in RNA alone, our investigation reveals the intricate roles of the ribosomal protein fragments (rPeptides) within the ribosomal core. This research highlights the significance of rPeptides in stability and coacervation of two distinct protoribosomal evolutionary stages. The 617nt 'big' protoribosome model, which associates with rPeptides specifically, exhibits a structurally defined and rigid nature, further stabilized by the peptides. In contrast, the 136nt 'small' model, previously linked to peptidyltransferase activity, displays greater structural flexibility. While this construct interacts with rPeptides with lower specificity, they induce coacervation of the 'small' protoribosome across a wide concentration range, which is concomitantly dependent on the RNA sequence and structure. Moreover, these conditions protect RNA from degradation. This phenomenon suggests a significant evolutionary advantage in the RNA-protein interaction at the early stages of ribosome evolution. The distinct properties of the two protoribosomal stages suggest that rPeptides initially provided compartmentalization and prevented RNA degradation, preceding the emergence of specific RNA-protein interactions crucial for the ribosomal structural integrity.
Návaznosti
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