J 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

EID Scopus

Klíčová slova anglicky

ORIGIN; PARAMETERS; PROTEINS; ACIDS; MODEL

Štítky

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

90242, velká výzkumná infrastruktura
Název: CIISB III