Publications
2009
Messmer M, Gaudry A, Sissler M, Florentz C
Pathology-related mutation A7526G (A9G) helps in the understanding of the 3D structural core of human mitochondrial tRNA(Asp) Article de journal
Dans: RNA, vol. 15, no. 8, p. 1462-1468, 2009, ISBN: 19535463, (1469-9001 (Electronic) Letter Research Support, Non-U.S. Gov't).
Résumé | Liens | BibTeX | Étiquettes: Asp/*chemistry/*genetics/metabolism Transfer RNA Aminoacylation/genetics, Binding Sites/genetics Humans Kinetics Mitochondrial Myopathies/genetics/metabolism/pathology Models, FLORENTZ, Missense Nucleic Acid Conformation RNA/*chemistry/*genetics/metabolism RNA, Molecular Mutation, SISSLER, Transfer, Unité ARN
@article{,
title = {Pathology-related mutation A7526G (A9G) helps in the understanding of the 3D structural core of human mitochondrial tRNA(Asp)},
author = {M Messmer and A Gaudry and M Sissler and C Florentz},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19535463},
isbn = {19535463},
year = {2009},
date = {2009-01-01},
journal = {RNA},
volume = {15},
number = {8},
pages = {1462-1468},
abstract = {More than 130 mutations in human mitochondrial tRNA (mt-tRNA) genes have been correlated with a variety of neurodegenerative and neuromuscular disorders. Their molecular impacts are of mosaic type, affecting various stages of tRNA biogenesis, structure, and/or functions in mt-translation. Knowledge of mammalian mt-tRNA structures per se remains scarce however. Primary and secondary structures deviate from classical tRNAs, while rules for three-dimensional (3D) folding are almost unknown. Here, we take advantage of a myopathy-related mutation A7526G (A9G) in mt-tRNA(Asp) to investigate both the primary molecular impact underlying the pathology and the role of nucleotide 9 in the network of 3D tertiary interactions. Experimental evidence is presented for existence of a 9-12-23 triple in human mt-tRNA(Asp) with a strongly conserved interaction scheme in mammalian mt-tRNAs. Mutation A7526G disrupts the triple interaction and in turn reduces aspartylation efficiency.},
note = {1469-9001 (Electronic)
Letter
Research Support, Non-U.S. Gov't},
keywords = {Asp/*chemistry/*genetics/metabolism Transfer RNA Aminoacylation/genetics, Binding Sites/genetics Humans Kinetics Mitochondrial Myopathies/genetics/metabolism/pathology Models, FLORENTZ, Missense Nucleic Acid Conformation RNA/*chemistry/*genetics/metabolism RNA, Molecular Mutation, SISSLER, Transfer, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
More than 130 mutations in human mitochondrial tRNA (mt-tRNA) genes have been correlated with a variety of neurodegenerative and neuromuscular disorders. Their molecular impacts are of mosaic type, affecting various stages of tRNA biogenesis, structure, and/or functions in mt-translation. Knowledge of mammalian mt-tRNA structures per se remains scarce however. Primary and secondary structures deviate from classical tRNAs, while rules for three-dimensional (3D) folding are almost unknown. Here, we take advantage of a myopathy-related mutation A7526G (A9G) in mt-tRNA(Asp) to investigate both the primary molecular impact underlying the pathology and the role of nucleotide 9 in the network of 3D tertiary interactions. Experimental evidence is presented for existence of a 9-12-23 triple in human mt-tRNA(Asp) with a strongly conserved interaction scheme in mammalian mt-tRNAs. Mutation A7526G disrupts the triple interaction and in turn reduces aspartylation efficiency.