Next Article in Journal
Evaluation of Stability of Amylose Inclusion Complexes Depending on Guest Polymers and Their Application to Supramolecular Polymeric Materials
Next Article in Special Issue
Protection of the Queuosine Biosynthesis Enzyme QueF from Irreversible Oxidation by a Conserved Intramolecular Disulfide
Previous Article in Journal / Special Issue
Factors That Shape Eukaryotic tRNAomes:  Processing, Modification and Anticodon–Codon Use
Article Menu

Export Article

Open AccessReview
Biomolecules 2017, 7(1), 27;

Biosynthesis of Sulfur-Containing tRNA Modifications: A Comparison of Bacterial, Archaeal, and Eukaryotic Pathways

Department of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803, USA
Author to whom correspondence should be addressed.
Academic Editor: Valérie de Crécy-Lagard
Received: 1 February 2017 / Revised: 3 March 2017 / Accepted: 6 March 2017 / Published: 11 March 2017
(This article belongs to the Collection RNA Modifications)
PDF [2508 KB, uploaded 11 March 2017]


Post-translational tRNA modifications have very broad diversity and are present in all domains of life. They are important for proper tRNA functions. In this review, we emphasize the recent advances on the biosynthesis of sulfur-containing tRNA nucleosides including the 2-thiouridine (s2U) derivatives, 4-thiouridine (s4U), 2-thiocytidine (s2C), and 2-methylthioadenosine (ms2A). Their biosynthetic pathways have two major types depending on the requirement of iron–sulfur (Fe–S) clusters. In all cases, the first step in bacteria and eukaryotes is to activate the sulfur atom of free l-cysteine by cysteine desulfurases, generating a persulfide (R-S-SH) group. In some archaea, a cysteine desulfurase is missing. The following steps of the bacterial s2U and s4U formation are Fe–S cluster independent, and the activated sulfur is transferred by persulfide-carrier proteins. By contrast, the biosynthesis of bacterial s2C and ms2A require Fe–S cluster dependent enzymes. A recent study shows that the archaeal s4U synthetase (ThiI) and the eukaryotic cytosolic 2-thiouridine synthetase (Ncs6) are Fe–S enzymes; this expands the role of Fe–S enzymes in tRNA thiolation to the Archaea and Eukarya domains. The detailed reaction mechanisms of Fe–S cluster depend s2U and s4U formation await further investigations. View Full-Text
Keywords: tRNA modification; sulfur; iron–sulfur cluster; translation tRNA modification; sulfur; iron–sulfur cluster; translation

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Čavužić, M.; Liu, Y. Biosynthesis of Sulfur-Containing tRNA Modifications: A Comparison of Bacterial, Archaeal, and Eukaryotic Pathways. Biomolecules 2017, 7, 27.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Biomolecules EISSN 2218-273X Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top