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Imino chemical shift assignments of tRNA, tRNA and tRNA from Escherichia coli.

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Expression génétique microbienne, Université Paris Cité, CNRS, Institut de biologie physico-chimique, IBPC, 13 rue Pierre et Marie Curie, Paris, 75005, France.

Transfer RNAs (tRNAs) are an essential component of the protein synthesis machinery. In order to accomplish their cellular functions, tRNAs go through a highly controlled biogenesis process leading to the production of correctly folded tRNAs. tRNAs in solution adopt the characteristic L-shape form, a stable tertiary conformation imperative for the cellular stability of tRNAs, their thermotolerance, their interaction with protein and RNA complexes and their activity in the translation process.

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Uridine residues present at the wobble position of eukaryotic cytosolic tRNAs often carry a 5-carbamoylmethyl (ncm), 5-methoxycarbonylmethyl (mcm), or 5-methoxycarbonylhydroxymethyl (mchm) side-chain. The presence of these side-chains allows proper pairing with cognate codons, and they are particularly important in tRNA species where the U residue is also modified with a 2-thio (s) group. The first step in the synthesis of the ncm, mcm, and mchm side-chains is dependent on the six-subunit Elongator complex, whereas the thiolation of the 2-position is catalyzed by the Ncs6/Ncs2 complex.

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Small molecules as ligands target multifunctional ribonucleic acids (RNA) for therapeutic engagement. This study explores how the anticancer DNA intercalator harmine interacts various motifs of RNAs, including the single-stranded A-form poly (rA), the clover leaf tRNA, and the double-stranded A-form poly (rC)-poly (rG). Harmine showed the affinity to the polynucleotides in the order, poly (rA) > tRNA > poly (rC)·poly (rG).

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Identification of Amino Acids in Trm734 Required for 2'--Methylation of the tRNA Wobble Residue.

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Department of Chemistry & Biochemistry, Dorothy Westerman Herrmann Science Center (SC), Room 204F, Northern Kentucky University, Highland Heights, Kentucky 41076, United States of America.

All organisms methylate their nucleic acids, and this methylation is critical for proper gene expression at both the transcriptional and translational levels. For proper translation in eukaryotes, 2'--methylation of C (Cm) and G (Gm) in the anticodon loop of tRNA is critical, with defects in these modifications associated with human disease. In yeast, Cm is formed by an enzyme that consists of the methyltransferase Trm7 in complex with the auxiliary protein Trm732, and Gm is formed by an enzyme that consists of Trm7 in complex with Trm734.

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Post-transcriptional modifications in RNA can significantly impact their structure and function. In particular, transfer RNAs (tRNAs) are heavily modified, with around 100 different naturally occurring nucleotide modifications contributing to codon bias and decoding efficiency. Here, we describe our efforts to investigate the impact of RNA modifications on the structure and stability of tRNA Phenylalanine (tRNA ) from S.

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