PMID:7523371
| Citation |
Raben, N, Nichols, R, Dohlman, J, McPhie, P, Sridhar, V, Hyde, C, Leff, R and Plotz, P (1994) A motif in human histidyl-tRNA synthetase which is shared among several aminoacyl-tRNA synthetases is a coiled-coil that is essential for enzymatic activity and contains the major autoantigenic epitope. J. Biol. Chem. 269:24277-83 |
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| Abstract |
In myositis, disease-specific autoantibodies may be directed against an aminoacyl-tRNA synthetase, usually histidyl-tRNA synthetase. To explore the basis for this phenomenon, we have made recombinant histidyl-tRNA synthetase in the baculovirus system. It was enzymatically active and recognized by human autoantibodies. A truncated protein lacking the first 60 amino acids was inactive as an antigen and as an enzyme. This region is within the first two exons, is predicted to have a coiled-coil configuration, and is found in some other synthetases but not in Escherichia coli or yeast histidyl-tRNA synthetase. Circular dichroism showed that the peptides from this region (amino acids 1-60 and 1-47) have the predicted high alpha-helical content, but smaller fragments (1-30, 14-45, and 31-60) do not. The peptides with a high alpha-helical content could inhibit autoantibodies almost completely, whereas the smaller peptides were unable to do so. The amino acid sequence of this coiled-coil domain in human histidyl-tRNA synthetase resembles the sequence of the extended this coiled-coil arm near the NH2 terminus of bacterial seryl-tRNA synthetase as well as similar regions in some eukaryotic aminoacyl-tRNA synthetases, raising the possibility that this domain serves a similar tRNA-stabilizing role and has been preserved from a common ancestor. |
| Links | |
| Keywords |
Amino Acid Sequence; Amino Acyl-tRNA Synthetases/chemistry; Animals; Autoantibodies/blood; Autoantibodies/immunology; Autoantigens/chemistry; Autoantigens/immunology; Baculoviridae/genetics; Cells, Cultured; Epitopes/chemistry; Epitopes/immunology; Exons; Histidine-tRNA Ligase/chemistry; Histidine-tRNA Ligase/genetics; Histidine-tRNA Ligase/immunology; Histidine-tRNA Ligase/isolation & purification; Humans; Molecular Sequence Data; Moths; Protein Conformation; Recombinant Proteins |
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