• search hit 4 of 10
Back to Result List

Shared sulfur mobilization routes for tRNA thiolation and molybdenum cofactor biosynthesis in prokaryotes and eukaryotes

  • 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 xm(5)s(2)U 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 surprisingModifications 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 xm(5)s(2)U 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.show moreshow less

Download full text files

  • pmnr1015.pdfeng
    (7368KB)

    SHA-512:dea0bfeeb904f2f871e68c15eb3a58a872f777f485c66d536865a5f9330e898ed7456ed64d85a505574217e0f97ff2adf2c446658230a310cf4e3f7f4de403ad

Export metadata

Additional Services

Search Google Scholar Statistics
Metadaten
Author details:Silke LeimkühlerORCiDGND, Martin BühningGND, Lena Beilschmidt
URN:urn:nbn:de:kobv:517-opus4-475011
DOI:https://doi.org/10.25932/publishup-47501
ISSN:1866-8372
Title of parent work (German):Postprints der Universität Potsdam : Mathematisch Naturwissenschaftliche Reihe
Publication series (Volume number):Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe (1015)
Publication type:Postprint
Language:English
Date of first publication:2020/11/12
Publication year:2017
Publishing institution:Universität Potsdam
Release date:2020/11/12
Tag:l-cysteine desulfurase; molybdenum cofactor; persulfide; sulfurtransferase; tRNA; thiocarboxylate; thionucleosides
Issue:1015
Number of pages:22
Source:Biomolecules 7 (2017) 1, Art. 5 DOI: 10.3390/biom7010005
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
DDC classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Peer review:Referiert
Publishing method:Open Access / Green Open-Access
License (German):License LogoCC-BY - Namensnennung 4.0 International
External remark:Bibliographieeintrag der Originalveröffentlichung/Quelle
Accept ✔
This website uses technically necessary session cookies. By continuing to use the website, you agree to this. You can find our privacy policy here.