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Sulfur Modifications of theWobble U34 in tRNAs and their Intracellular Localization in Eukaryotic Cells.

Authors :
Yumi Nakai
Takato Yano
Masato Nakai
Source :
Biomolecules (2218-273X). Mar2017, Vol. 7 Issue 1, p17. 13p.
Publication Year :
2017

Abstract

The wobble uridine (U34) of transfer RNAs (tRNAs) for two-box codon recognition, i.e., tRNALys UUU, tRNAGlu UUC, and tRNAGln UUG, harbor a sulfur- (thio-) and a methyl-derivative structure at the second and fifth positions of U34, respectively. Both modifications are necessary to construct the proper anticodon loop structure and to enable them to exert their functions in translation. Thio-modification of U34 (s2U34) is found in both cytosolic tRNAs (cy-tRNAs) and mitochondrial tRNAs (mt-tRNAs). Although L-cysteine desulfurase is required in both cases, subsequent sulfur transfer pathways to cy-tRNAs and mt-tRNAs are different due to their distinct intracellular locations. The s2U34 formation in cy-tRNAs involves a sulfur delivery system required for the biosynthesis of iron-sulfur (Fe/S) clusters and certain resultant Fe/S proteins. This review addresses presumed sulfur delivery pathways for the s2U34 formation in distinct intracellular locations, especially that for cy-tRNAs in comparison with that for mt-tRNAs. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
2218273X
Volume :
7
Issue :
1
Database :
Academic Search Index
Journal :
Biomolecules (2218-273X)
Publication Type :
Academic Journal
Accession number :
122052221
Full Text :
https://doi.org/10.3390/biom7010017