TudS desulfidases recycle 4-thiouridine-5’-monophosphate at a catalytic [4Fe-4S] cluster - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Communications Biology Année : 2023

TudS desulfidases recycle 4-thiouridine-5’-monophosphate at a catalytic [4Fe-4S] cluster

Résumé

In all domains of life, transfer RNAs (tRNAs) contain post-transcriptionally sulfur-modified nucleosides such as 2-and 4-thiouridine. We have previously reported that a recombinant [4Fe-4S] cluster-containing bacterial desulfidase (TudS) from an uncultured bacterium catalyzes the desulfuration of 2-and 4-thiouracil via a [4Fe-5S] cluster intermediate. However, the in vivo function of TudS enzymes has remained unclear and direct evidence for substrate binding to the [4Fe-4S] cluster during catalysis was lacking. Here, we provide kinetic evidence that 4-thiouridine-5'-monophosphate rather than sulfurated tRNA, thiouracil, thiouridine or 4-thiouridine-5'-triphosphate is the preferred substrate of TudS. The occurrence of sulfur-and substrate-bound catalytic intermediates was uncovered from the observed switch of the S = 3/2 spin state of the catalytic [4Fe-4S] cluster to a S = 1/2 spin state upon substrate addition. We show that a putative gene product from Pseudomonas putida KT2440 acts as a TudS desulfidase in vivo and conclude that TudS-like enzymes are widespread desulfidases involved in recycling and detoxifying tRNA-derived 4-thiouridine monophosphate nucleosides for RNA synthesis.
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hal-04304111 , version 1 (24-11-2023)

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Jonathan Fuchs, Rapolas Jamontas, Maren Hellen Hoock, Jonathan Oltmanns, Béatrice Golinelli-Pimpaneau, et al.. TudS desulfidases recycle 4-thiouridine-5’-monophosphate at a catalytic [4Fe-4S] cluster. Communications Biology, 2023, 6, pp.1092. ⟨10.1038/s42003-023-05450-5⟩. ⟨hal-04304111⟩
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