Interactions of bovine mitochondrial phenylalanyl-tRNA with ribosomes and elongation factors from mitochondria and bacteria

Higher-order structure of bovine mitochondrial tRNASerUGA: chemical modification and computer modeling

“…The concept of their paper and that of our own are exactly the same, although they were formulated independently. It should be noted, however, that Steinberg and Cedergren reached their conclusion through theoretical interpretation of several kinds of atypical mitochondrial tRNA gene sequences, whereas we reached ours through the systematic interpretation of our already published data (9,11,12,14,24) and the experimental data presented here.…”

“…A recent report on the enzymatic and chemical probing of bovine mt tRNAPhe suggests that the canonical extra loop/D arm interactions preserve the L-shape, higher-order structure, although tRNAPhe lacks the D loop/T loop interactions (9). It has also been found that the tertiary structure of another serine isoacceptor tRNA of bovine mitochondria-tRNAserGCU-could be modeled so as to conform to this condition (13, and our unpublished results), under which all the mt tRNAs with their various structural variations would be able to function in the mt translation system (24). Note After the manuscript for this paper had been completed and submitted for publication, a paper by Steinberg and Cedergren closely related to our present theme was published (31).…”

Codon-specific translational defect caused by a wobble modification deficiency in mutant tRNA from a human mitochondrial disease

“…In the case of the nonenzymatic ribosomal A-site-binding experiment, the aminoacylation level of the two aminoacylated tRNAs was almost equal (88% for WT and 87% for operated), so it hardly became a problem. We used E. coli ribosome instead of the human mitochondrial counterpart in the binding assay, because the precise condition for the assay using E. coli ribosome is completely established and it has been shown that mt tRNA enables translation to proceed on E. coli ribosome and, conversely, that E. coli tRNA dose likewise on mt ribosome (39,40).…”

Pathogenic mechanism of a human mitochondrial tRNA Phe mutation associated with myoclonic epilepsy with ragged red fibers syndrome

“…Thus, whereas the CϫA mismatch at the third position of the codon-anticodon helix is well tolerated, a CϫA mismatch at the first position is not. It has been shown that the E. coli ribosome can use mitochondrial tRNAs, and it is likely that the mitochondrial ribosome is able to use bacterial tRNAs as well (51,52), reflecting the inherent similarity between bacterial and mitochondrial ribosomes. Given these various considerations, it is reasonable to envision that the G34A mutation of hmt-tRNA Phe would not appreciably affect decoding of Phe codons in vivo.…”