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Cloning and Characterization of cDNA Encoding the Rabbit tRNA-Guanine Transglycosylase 60-Kilodalton Subunit

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 w...

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Bibliographic Details
Published in:Archives of biochemistry and biophysics 1996-02, Vol.326 (1), p.1-7
Main Authors: Deshpande, Kathryn L., Seubert, Patricia H., Tillman, David M., Farkas, Walter R., Katze, Jon R.
Format: Article
Language:English
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Summary: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,Nature366, 313–319), especially with sequence elements that include conserved Cys and His residues.
ISSN:0003-9861
1096-0384
DOI:10.1006/abbi.1996.0039