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Iron–sulfur biology invades tRNA modification: the case of U34 sulfuration

Abstract : Sulfuration of uridine 34 in the anticodon of tRNAs is conserved in the three domains of life, guaranteeing fidelity of protein translation. In eubacteria, it is catalyzed by MnmA-type enzymes, which were previously concluded not to depend on an iron-sulfur [Fe-S] cluster. However, we report here spectroscopic and iron / sulfur analysis, as well as in vitrocatalytic assays and site-directed mutagenesis studies unambiguously showing that MnmA from Escherichia coli can bind a [4Fe-4S] cluster, which is essential for sulfuration of U34-tRNA. We propose that the cluster serves to bind and activate hydrosulfide for nucleophilic attack on the adenylated nucleoside. Intriguingly, we found that E. colicells retain s 2 U34 biosynthesis in the iscUA sufABCDSE strain, lacking functional ISC and SUF [Fe-S] cluster assembly machineries, thus suggesting an original and yet undescribed way of maturation of MnmA. Moreover, we report genetic analysis showing the importance of MnmA for sustaining oxidative stress.
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Contributor : Béatrice Golinelli-Pimpaneau <>
Submitted on : Thursday, April 15, 2021 - 11:52:01 AM
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Jingjing Zhou, Marine Lénon, Jean-Luc Ravanat, Nadia Touati, Christophe Velours, et al.. Iron–sulfur biology invades tRNA modification: the case of U34 sulfuration. Nucleic Acids Research, Oxford University Press, 2021, 49 (7), pp.3997-4007. ⟨10.1093/nar/gkab138⟩. ⟨hal-03198943⟩



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