Cloning and characterization of cDNA encoding a human arginyl-tRNA synthetase.
Arginyl-tRNA synthetase (ArgRS) plays a key role in protein synthesis as part of a multienzyme complex with a number of other aminoacyl-tRNA synthetase (aaRS) enzymes. We have isolated a full-length cDNA encoding ArgRS as part of a project on complementation of radiosensitivity in human cells with an Epstein-Barr Virus (EBV) vector-based human cDNA library. DNA sequence analysis identified an open reading frame of 1983 nucleotides with 87% homology to other mammalian ArgRS genes. The deduced amino acid (aa) sequence (661 aa) showed 87.7% identity to the Chinese hamster ovary (CHO) enzyme and 37.7% identity to the homologous Escherichia coli enzyme. Northern blot analysis revealed the presence of a single mRNA species of approx. 2.2 kb. The results described here demonstrate that ArgRS is highly conserved in mammalian cells and confirm the presence of a hydrophobic N-terminal region in the higher-molecular-weight complexed form of ArgRS.
Girjes
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AA
Queensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Brisbane, Australia.
Hobson
K
K
Chen
P
P
Lavin
M F
MF
D000595:Amino Acid Sequence; D000818:Animals; D001126:Arginine-tRNA Ligase / Q000096:biosynthesis* / Q000235:genetics*; D001483:Base Sequence; D016466:CHO Cells; D002460:Cell Line; D016384:Consensus Sequence; D006224:Cricetinae; D018076:DNA, Complementary; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D015723:Gene Library; D005822:Genetic Vectors; D004854:Herpesvirus 4, Human; D015186:Hominidae / Q000235:genetics*; D006801:Humans; D008099:Liver / Q000201:enzymology; D008322:Mammals; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D011836:Radiation Tolerance; D051381:Rats; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid
D018076:DNA, Complementary; D001126:Arginine-tRNA Ligase