期刊
NUCLEIC ACIDS RESEARCH
卷 49, 期 14, 页码 8247-8260出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkab567
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资金
- National Institutes of Health [GM058843, GM132254, GM084065-11]
- Czech Science Foundation [15-21450Y, 20-11585S]
- ERDF/ESF project Centre for Research of Pathogenicity and Virulence of Parasites [CZ.02.1.01/0.0/0.0/16 019/0000759]
- University of South Bohemia [036/2017/P]
- Biology Centre, Czech Academy of Sciences, Ceske Bude.jovice, Czech Republic
Research revealed that in the protozoan parasite Trypanosoma brucei, Q-modified tRNAs have a preference for specific codons, which is crucial for mitochondrial protein synthesis and overall protein synthesis regulation.
Transfer RNAs (tRNAs) are key players in protein synthesis. To be fully active, tRNAs undergo extensive post-transcriptional modifications, including queuosine (Q), a hypermodified 7-deaza-guanosine present in the anticodon of several tRNAs in bacteria and eukarya. Here, molecular and biochemical approaches revealed that in the protozoan parasite Trypanosoma brucei, Q-containing tRNAs have a preference for the U-ending codons for asparagine, aspartate, tyrosine and histidine, analogous to what has been described in other systems. However, since a lack of tRNA genes in T. brucei mitochondria makes it essential to import a complete set from the cytoplasm, we surprisingly found that Q-modified tRNAs are preferentially imported over their unmodified counter-parts. In turn, their absence from mitochondria has a pronounced effect on organellar translation and affects function. Although Q modification in T. brucei is globally important for codon selection, it is more so for mitochondrial protein synthesis. These results provide a unique example of the combined regulatory effect of codon usage and wobble modifications on protein synthesis; all driven by tRNA intracellular transport dynamics.
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