An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase.
Interferon gamma induces expression of a protein termed IFP 53 according to its molecular weight of 53 kDa. IFP 53 shows significant sequence homology to rabbit peptide chain release factor as well as to bovine tryptophanyl-tRNA synthetase. IFP 53 has been shown to possess release factor activity for the UGA stop codon. We demonstrate here, by using a recombinant IFP 53 fusion protein, that IFP 53 tryptophanylates tRNA. These data indicate that IFP 53 is a protein with two activities: peptide chain termination and aminoacylation.
Medical School Hannover, Institute for Medical Microbiology, Germany.
F C
FC
Bange
T
T
Flohr
U
U
Buwitt
E C
EC
Böttger
D000215:Acylation; D000595:Amino Acid Sequence; D015153:Blotting, Western; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004790:Enzyme Induction; D006367:HeLa Cells; D006801:Humans; D007372:Interferons / Q000494:pharmacology; D008969:Molecular Sequence Data; D011993:Recombinant Fusion Proteins; D012689:Sequence Homology, Nucleic Acid; D014369:Tryptophan-tRNA Ligase / Q000096:biosynthesis / Q000502:physiology*
D011993:Recombinant Fusion Proteins; D007372:Interferons; D014369:Tryptophan-tRNA Ligase; C073175:WARS1 protein, human