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The interplay between peptides and RNA is critical for protoribosome compartmentalization and stability

S. Codispoti, T. Yamaguchi, M. Makarov, VG. Giacobelli, M. Mašek, MH. Kolář, AC. Sanchez Rocha, K. Fujishima, G. Zanchetta, K. Hlouchová

. 2024 ; 52 (20) : 12689-12700. [pub] 20241111

Jazyk angličtina Země Anglie, Velká Británie

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/bmc25003485

Grantová podpora
Charles University
TOYOBO Biotechnology Foundation
RGEC27/2023]; Human Frontier Science Program
[4EU+/22/F4/25 Univerzita Karlova v Praze
AB301003, NINS
LM2023042 Ministerstvo Školství, Mládeže a Tělovýchovy
CZ.02.1.01/0.0/0.0/18_046/0015974 European Regional Development Fund
21J12128 JSPS

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.

Citace poskytuje Crossref.org

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