Backbone and side chain NMR assignments for the ribosome maturation factor P (RimP) from Staphylococcus aureus.

Fiche publication

Date publication

septembre 2022

Journal

Biomolecular NMR assignments

Auteurs

Membres identifiés du Cancéropôle Est :
Dr YUSUPOV Marat

Tous les auteurs :
Garaeva NS, Bikmullin AG, Fatkhullin BF, Validov SZ, Keiffer B, Yusupov MM, Usachev KS

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/36070063

Résumé

The ribosomal maturation factor (RimP) is a 17.7 kDa protein and is the assembly factor of the 30S subunit. RimP is essential for efficient processing of 16S rRNA and maturation (assembly) of the 30S ribosome. It was suggested that RimP takes part in stabilization of the central pseudoknot at the early stages of the 30S subunit maturation, and this process may occur before the head domain assembly and later stages of the 30S assembly, but the mechanism of this interaction is still not fully understood. Here we report the assignment of the H, C and N chemical shift in the backbone and side chains of RimP from Staphylococcus aureus. Analysis of chemical shifts of the main chain using TALOS + suggests that the RimP contains eight β-strands and three α-helices with the topology α1-β1-β2-α2- β3- α3- β4- β5- β6- β7- β8. Structural studies of RimP and its complex with the ribosome by integrated structural biology approaches (NMR spectroscopy, X-ray diffraction analysis and cryoelectron microscopy) will allow further screening of highly selective inhibitors of the translation of S. aureus.