Structural aspects of RimP binding on small ribosomal subunit from Staphylococcus aureus

Garaeva, Nataliia; Fatkhullin, Bulat; Murzakhanov, Fadis; Gafurov, Marat; Golubev, Alexander; Bikmullin, Aydar; Glazyrin, Maxim; Kieffer, Bruno; Jenner, Lasse; Klochkov, Vladimir; Aganov, Albert; Rogachev, Andrey; Ivankov, Oleksandr; Validov, Shamil; Yusupov, Marat; Usachev, Konstantin

doi:10.1016/j.str.2023.10.014

Cited by 1 publication

(3 citation statements)

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“…1 ; Jahagirdar et al 2020 ; Schedlbauer et al 2021 ). Recently, the same rRNA rearrangement was observed in Staphylococcus aureus ( Garaeva et al 2024 ), suggesting that this conformational switch is widespread in bacteria.…”

Section: Introductionmentioning

confidence: 53%

“…To form hALT, the 3' end of the 16S flips across the subunit and occupies the mRNA Warner 4 entry channel, occluding the P and A codons (Figure 1) (Jahagirdar et al 2020;Schedlbauer et al 2021). Recently, the same rRNA rearrangement was observed in Staphylococcus aureus (Garaeva et al 2024), suggesting that this conformational switch is widespread in bacteria.…”

Section: Introductionmentioning

confidence: 57%

“…A number of assembly factors, including RNP-binding proteins, modification enzymes, and GTPases, facilitate the process and/or prevent immature particles from participating in translation. Interestingly, assembly factor RimP will induce the active-to-inactive transition in vitro with E. coli and S. aureus subunits in the presence of high (10 mM) Mg 2+ ( Schedlbauer et al 2021 ; Garaeva et al 2024 ). Moreover, it has been independently shown that Δ ksgA cells accumulate pre-30S particles that adopt the inactive state ( Sun et al 2023 ).…”

Section: Introductionmentioning

confidence: 99%

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Contribution of an alternative 16S rRNA helix to biogenesis of the 30S subunit of the ribosome

Warner,

Fredrick

2024

RNA

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30S subunits become inactive upon exposure to low Mg2+ concentration, due to a reversible conformational change that entails nucleotides (nt) in the neck helix (h28) and 3’ tail of 16S rRNA. This active-to-inactive transition involves partial unwinding of h28 and re-pairing of nt 921-923 with nt 1532-1534, which requires flipping of the 3’ tail by ~180 degrees. Growing evidence suggests that immature 30S particles adopt the inactive conformation in the cell, and transition to the active state occurs at a late stage of maturation. Here, we target nucleotides that form the alternative helix (hALT) of the inactive state. Using an orthogonal ribosome system, we find that disruption of hALT decreases translation activity in the cell modestly, by ~2-fold, without compromising ribosome fidelity. Ribosomes carrying substitutions at positions 1532-1533 support growth of E. coli strain Δ7 prrn (which carries a single rRNA operon), albeit at rates 10-20% slower than wild-type ribosomes. These mutant Δ7 prrn strains accumulate free 30S particles and precursor 17S rRNA, indicative of biogenesis defects. Analysis of purified control and mutant subunits suggests that hALT stabilizes the inactive state by 1.2 kcal/mol with little-to-no impact on the active state or the transition state of conversion.

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Section: Introductionmentioning

confidence: 53%

Section: Introductionmentioning

confidence: 57%