Toward the Full Set of Human Mitochondrial Aminoacyl-tRNA Synthetases: Characterization of AspRS and TyrRS †

Autor: Aurélie Fender, Luc Bonnefond, Richard Giegé, Catherine Florentz, Marie Sissler, Joëlle Rudinger-Thirion
Přispěvatelé: Centre National de la Recherche Scientifique (CNRS)
Jazyk: angličtina
Rok vydání: 2005
Předmět:
Mitochondrial DNA
Sequence analysis
MESH: Mitochondria
[SDV]Life Sciences [q-bio]
Aspartate-tRNA Ligase
Molecular Sequence Data
MESH: RNA
Transfer
Asp

MESH: Amino Acid Sequence
Mitochondrion
Biology
MESH: Base Sequence
MESH: Databases
Nucleic Acid

Biochemistry
environment and public health
MESH: Recombinant Proteins
03 medical and health sciences
chemistry.chemical_compound
0302 clinical medicine
Tyrosine-tRNA Ligase
MESH: Tyrosine-tRNA Ligase
MESH: RNA
Transfer
Tyr

Humans
MESH: Cloning
Molecular

Amino Acid Sequence
MESH: Aspartate-tRNA Ligase
Cloning
Molecular

Gene
Peptide sequence
030304 developmental biology
Genetics
RNA
Transfer
Asp

0303 health sciences
MESH: Humans
MESH: Molecular Sequence Data
Base Sequence
Aminoacyl tRNA synthetase
Computational Biology
RNA
Recombinant Proteins
Mitochondria
RNA
Transfer
Tyr

MESH: Transfer RNA Aminoacylation
chemistry
Transfer RNA
Transfer RNA Aminoacylation
Databases
Nucleic Acid

030217 neurology & neurosurgery
MESH: Computational Biology
Zdroj: Biochemistry
Biochemistry, American Chemical Society, 2005, 44 (12), pp.4805-4816. ⟨10.1021/bi047527z⟩
ISSN: 0006-2960
1520-4995
DOI: 10.1021/bi047527z⟩
Popis: International audience; The human mitochondrion possesses a translational machinery devoted to the synthesis of 13 proteins. While the required tRNAs and rRNAs are produced by transcription of the mitochondrial genome, all other factors needed for protein synthesis are synthesized in the cytosol and imported. This is the case for aminoacyl-tRNA synthetases, the enzymes which esterify their cognate tRNA with the specific amino acid. The genes for the full set of cytosolic aaRSs are well defined, but only nine genes for mitochondrial synthetases are known. Here we describe the genes for human mitochondrial aspartyl- and tyrosyl-tRNA synthetases and the initial characterization of the enzymes. Both belong to the expected class of synthetases, have a dimeric organization, and aminoacylate Escherichia coli tRNAs as well as in vitro transcribed human mitochondrial tRNAs. Genes for the remaining missing synthetases were also found with the exception of glutaminyl-tRNA synthetase. Their sequence analysis confirms and further extends the view that, except for lysyl- and glycyl-tRNA synthetases, human mitochondrial and cytosolic enzymes are coded by two different sets of genes.
Databáze: OpenAIRE