Bacterial wobble modifications of NNA‐decoding tRNAs
Autor: | Rebecca W. Alexander, Emil M. Nilsson |
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Rok vydání: | 2019 |
Předmět: |
0301 basic medicine
Clinical Biochemistry Bacillus Computational biology Wobble base pair environment and public health Biochemistry Ribosome Article Mycobacterium Amino Acyl-tRNA Synthetases 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine RNA Transfer Anticodon Escherichia coli Genetics medicine TRNA aminoacylation RNA Processing Post-Transcriptional Codon Inosine Base Pairing Molecular Biology Bacteria Models Genetic Lysine Thermus thermophilus RNA Cell Biology Pyrimidine Nucleosides Genetic code 030104 developmental biology chemistry Genetic Code Protein Biosynthesis 030220 oncology & carcinogenesis Transfer RNA Lysidine Ribosomes medicine.drug |
Zdroj: | IUBMB Life |
ISSN: | 1521-6551 1521-6543 1158-1166 |
DOI: | 10.1002/iub.2120 |
Popis: | Nucleotides of transfer RNAs (tRNAs) are highly modified, particularly at the anticodon. Bacterial tRNAs that read A-ending codons are especially notable. The U34 nucleotide canonically present in these tRNAs is modified by a wide range of complex chemical constituents. An additional two A-ending codons are not read by U34-containing tRNAs but are accommodated by either inosine or lysidine at the wobble position (I34 or L34). The structural basis for many N34 modifications in both tRNA aminoacylation and ribosome decoding has been elucidated, and evolutionary conservation of modifying enzymes is also becoming clearer. Here we present a brief review of the structure, function, and conservation of wobble modifications in tRNAs that translate A-ending codons. © 2019 IUBMB Life, 2019 © 2019 IUBMB Life, 71(8):1158-1166, 2019. |
Databáze: | OpenAIRE |
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