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Molecular cloning and characterization of an interferon induced human cDNA with sequence homology to a mammalian peptide chain release factor.
Author(s) -
Buwitt U.,
Flohr T.,
Böttger E.C.
Publication year - 1992
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1992.tb05079.x
Subject(s) - microbiology and biotechnology , complementary dna , biology , cloning (programming) , homology (biology) , genetics , gene , computer science , programming language
Here we report the molecular cloning of several related human cDNAs from which a full‐length sequence can be determined. The cDNAs encode a 2.8 kb mRNA that is strongly induced by interferon (IFN) gamma and the expression of which is not cell‐restricted but observed in fibroblasts, macrophages and epithelial cells. The deduced amino acid sequence predicts a protein of 471 amino acids with high sequence similarity to a previously identified rabbit peptide chain release factor. Functional studies to demonstrate release factor activity showed that the protein encoded by this cDNA inhibited the readthrough activity of a yeast UGA suppressor tRNA in an in vitro translation system. The identification of this novel cDNA implies that translational control by IFN induced proteins may not be restricted to the initial steps of protein synthesis but may also act by regulation of peptide chain termination.