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Structure-based mechanistic insights into catalysis by tRNA thiolation enzymes

Abstract : In all domains of life, ribonucleic acid (RNA) maturation includes post-transcriptional chemical modifications of nucleosides. Many sulfur-containing nucleosides have been identified in transfer RNAs (tRNAs), such as the derivatives of 2-thiouridine (s 2 U), 4-thiouridine (s 4 U), 2-thiocytidine (s 2 C), 2-methylthioadenosine (ms 2 A). These modifications are essential for accurate and efficient translation of the genetic code from messenger RNA (mRNA) for protein synthesis. This review summarizes the recent discoveries concerning the mechanistic and structural characterization of tRNA thiolation enzymes that catalyze the non-redox substitution of oxygen for sulfur in nucleosides. Two mechanisms have been described. One involves persulfide formation on catalytic cysteines, while the other uses a [4Fe-4S] cluster, chelated by three conserved cysteines only, as a sulfur carrier. 2
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https://hal.archives-ouvertes.fr/hal-02945297
Contributor : Béatrice Golinelli-Pimpaneau <>
Submitted on : Tuesday, September 22, 2020 - 10:53:31 AM
Last modification on : Thursday, January 7, 2021 - 4:36:05 PM
Long-term archiving on: : Friday, December 4, 2020 - 6:30:23 PM

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Ornella Bimai, Simon Arragain, Béatrice Golinelli-Pimpaneau. Structure-based mechanistic insights into catalysis by tRNA thiolation enzymes. Current Opinion in Structural Biology, Elsevier, 2020, 65, pp.69-78. ⟨10.1016/j.sbi.2020.06.002⟩. ⟨hal-02945297⟩

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