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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.zeige mehrzeige weniger

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Metadaten
Verfasserangaben: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
Titel des übergeordneten Werks (Deutsch):Postprints der Universität Potsdam : Mathematisch Naturwissenschaftliche Reihe
Schriftenreihe (Bandnummer):Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe (1015)
Publikationstyp:Postprint
Sprache:Englisch
Datum der Erstveröffentlichung:12.11.2020
Erscheinungsjahr:2017
Veröffentlichende Institution:Universität Potsdam
Datum der Freischaltung:12.11.2020
Freies Schlagwort / Tag:l-cysteine desulfurase; molybdenum cofactor; persulfide; sulfurtransferase; tRNA; thiocarboxylate; thionucleosides
Ausgabe:1015
Seitenanzahl:22
Quelle:Biomolecules 7 (2017) 1, Art. 5 DOI: 10.3390/biom7010005
Organisationseinheiten:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
DDC-Klassifikation:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Peer Review:Referiert
Publikationsweg:Open Access / Green Open-Access
Lizenz (Deutsch):License LogoCC-BY - Namensnennung 4.0 International
Externe Anmerkung:Bibliographieeintrag der Originalveröffentlichung/Quelle
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