Next Article in Journal / Special Issue
Critical Minireview: The Fate of tRNACys during Oxidative Stress in Bacillus subtilis
Previous Article in Journal
Acknowledgement to Reviewers of Biomolecules in 2016
Previous Article in Special Issue
CoverageAnalyzer (CAn): A Tool for Inspection of Modification Signatures in RNA Sequencing Profiles
Article Menu

Export Article

Open AccessReview
Biomolecules 2017, 7(1), 5; doi:10.3390/biom7010005

Shared Sulfur Mobilization Routes for tRNA Thiolation and Molybdenum Cofactor Biosynthesis in Prokaryotes and Eukaryotes

Department of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, 14476 Potsdam, Germany
*
Author to whom correspondence should be addressed.
Academic Editor: Valérie de Crécy-Lagard
Received: 8 December 2016 / Revised: 4 January 2017 / Accepted: 9 January 2017 / Published: 14 January 2017
(This article belongs to the Special Issue tRNA Modifications: Synthesis, Function and Beyond)
View Full-Text   |   Download PDF [5985 KB, uploaded 14 January 2017]   |  

Abstract

Modifications of transfer RNA (tRNA) have been shown to play critical roles in the biogenesis, metabolism, structural stability and function of RNA molecules, and the specific modifications of nucleobases with sulfur atoms in tRNA are present in pro- and eukaryotes. Here, especially the thiomodifications xm5s2U at the wobble position 34 in tRNAs for Lys, Gln and Glu, were suggested to have an important role during the translation process by ensuring accurate deciphering of the genetic code and by stabilization of the tRNA structure. The trafficking and delivery of sulfur nucleosides is a complex process carried out by sulfur relay systems involving numerous proteins, which not only deliver sulfur to the specific tRNAs but also to other sulfur-containing molecules including iron–sulfur clusters, thiamin, biotin, lipoic acid and molybdopterin (MPT). Among the biosynthesis of these sulfur-containing molecules, the biosynthesis of the molybdenum cofactor (Moco) and the synthesis of thio-modified tRNAs in particular show a surprising link by sharing protein components for sulfur mobilization in pro- and eukaryotes. View Full-Text
Keywords: tRNA; molybdenum cofactor; persulfide; thiocarboxylate; thionucleosides; sulfurtransferase; l-cysteine desulfurase tRNA; molybdenum cofactor; persulfide; thiocarboxylate; thionucleosides; sulfurtransferase; l-cysteine desulfurase
Figures

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).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Leimkühler, S.; Bühning, M.; Beilschmidt, L. Shared Sulfur Mobilization Routes for tRNA Thiolation and Molybdenum Cofactor Biosynthesis in Prokaryotes and Eukaryotes. Biomolecules 2017, 7, 5.

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

1

Comments

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