Cloning and Characterization of cDNA Encoding the Rabbit tRNA-Guanine Transglycosylase 60-Kilodalton Subunit
| Autor: | Walter R. Farkas, Jon R. Katze, Patricia H. Seubert, David M. Tillman, Kathryn L. Deshpande |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
DNA
Complementary Erythrocytes Guanine Protein subunit Molecular Sequence Data Biophysics Queuosine Biology Biochemistry chemistry.chemical_compound Complementary DNA Animals Amino Acid Sequence Pentosyltransferases Nucleoside Q Cloning Molecular Molecular Biology Base Sequence Queuine Molecular biology Open reading frame chemistry Transfer RNA Rabbits Sequence Alignment |
| Zdroj: | Archives of Biochemistry and Biophysics. 326:1-7 |
| ISSN: | 0003-9861 |
| DOI: | 10.1006/abbi.1996.0039 |
| Popis: | Eukaryotes synthesize queuosine (nucleoside Q) by the irreversible base-for-base exchange of queuine (Q base) for guanine at tRNA position 34, a reaction catalyzed by tRNA-guanine transglycosylase (TGT). The physiological role of Q remains unknown but the tRNA of tumor cells often is undermodified with respect to Q. Toward an understanding of the function of Q in normal and neoplastic cells we have isolated and characterized the cDNA for rabbit TGT. Rabbit erythrocyte TGT was reported previously to be a dimer of 60- and 43-kDa subunits (N. K. Howes and W. R. Farkas, 1978, J. Biol. Chem. 253, 9082-9078). Here we present the cDNA sequence for the apparent 60-kDa subunit; it contains an open reading frame encoding a 493-residue protein. The rabbit TGT 60-kDa subunit shares significant sequence similarity with the deubiquitinating enzyme family (F. R. Papa and M. Hochstrasser, 1993, nature 366, 313-319), especially with sequence elements that include conserved Cys and His residues. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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