Functional redundancy in tRNA dihydrouridylation - UFR de Chimie de Sorbonne-Université Access content directly
Journal Articles Nucleic Acids Research Year : 2024

Functional redundancy in tRNA dihydrouridylation

Damien Brégeon


Dihydrouridine (D) is a common modified base found predominantly in transfer RNA (tRNA). Despite its prevalence, the mechanisms underlying dihydrouridine biosynthesis, particularly in prokaryotes, have remained elusive. Here, we conducted a comprehensive investigation into D biosynthesis in Bacillus subtilis through a combination of genetic, biochemical, and epitranscriptomic approaches. Our findings reveal that B. subtilis relies on two FMN-dependent Dus-like flavoprotein homologs, namely DusB1 and DusB2, to introduce all D residues into its tRNAs. Notably, DusB1 exhibits multisite enzyme activity, enabling D formation at positions 17, 20, 20a and 47, while DusB2 specifically catalyzes D biosynthesis at positions 20 and 20a, showcasing a functional redundancy among modification enzymes. Extensive tRNA-wide D-mapping demonstrates that this functional redundancy impacts the majority of tRNAs, with DusB2 displaying a higher dihydrouridylation efficiency compared to DusB1. Interestingly, we found that BsDusB2 can function like a BsDusB1 when overexpressed in vivo and under increasing enzyme concentration in vitro. Furthermore, we establish the importance of the D modification for B. subtilis growth at suboptimal temperatures. Our study expands the understanding of D modifications in prokaryotes, highlighting the significance of functional redundancy in this process and its impact on bacterial growth and adaptation.
Fichier principal
Vignette du fichier
Revised Dus Bacillus subtilis For NAR final umarked (1).pdf (2.4 Mo) Télécharger le fichier
Origin Files produced by the author(s)

Dates and versions

hal-04614743 , version 1 (17-06-2024)



Claudia Sudol, Lea-Marie Kilz, Virginie Marchand, Quentin Thullier, Vincent Guérineau, et al.. Functional redundancy in tRNA dihydrouridylation. Nucleic Acids Research, 2024, 52 (10), pp.5880-5894. ⟨10.1093/nar/gkae325⟩. ⟨hal-04614743⟩
0 View
0 Download



Gmail Mastodon Facebook X LinkedIn More