Bange F C, Flohr T, Buwitt U, Böttger E C
Medical School Hannover, Institute for Medical Microbiology, Germany.
FEBS Lett. 1992 Mar 30;300(2):162-6. doi: 10.1016/0014-5793(92)80187-l.
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.
γ干扰素根据其53千道尔顿的分子量诱导一种名为IFP 53的蛋白质表达。IFP 53与兔肽链释放因子以及牛色氨酰-tRNA合成酶具有显著的序列同源性。已证明IFP 53对UGA终止密码子具有释放因子活性。我们在此通过使用重组IFP 53融合蛋白证明，IFP 53使tRNA色氨酰化。这些数据表明IFP 53是一种具有两种活性的蛋白质：肽链终止和氨酰化。
