| Title |
TudS desulfidases recycle 4-thiouridine-5’-monophosphate at a catalytic [4Fe-4S] cluster / |
| Authors |
Fuchs, Jonathan ; Jamontas, Rapolas ; Hoock, Maren Hellen ; Oltmanns, Jonathan ; Golinelli-Pimpaneau, Béatrice ; Schünemann, Volker ; Pierik, Antonio J ; Meškys, Rolandas ; Aučynaitė, Agota ; Boll, Matthias |
| DOI |
10.1038/s42003-023-05450-5 |
| Full Text |
|
| Is Part of |
Communications biology.. Nature Research. 2023, vol. 6, iss. 1, art. no. 1092, p. [1-11].. eISSN 2399-3642 |
| Abstract [eng] |
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. |
| Published |
Nature Research |
| Type |
Journal article |
| Language |
English |
| Publication date |
2023 |
| CC license |
|
