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Nucleic Acids Research, 1988, Vol. 16, No. 12 5391-5406
© 1988

Articles

The core region of human glutaminyl-tRNA synthetase homologies with the Escherichia coti and yeast enzymes

Pia Thommes, Radegunde Fett, Beate Schray, Norbert Kunze and Rolf Knippers

Fakultat für Biologie, Universitat Konstanz D-7750 Konstanz, FRG

Received March 29, 1988. Revised May 20, 1988. Accepted May 20, 1988.

We have isolated from a Lambda-gt 11 library a human cDNA clone with one open reading frame of about 2400 bases. A stretch of about 350 amino acids in the deduced amino acid sequence is up to 40 percent identical with parts of the known amino acid sequences of E.coli and yeast glutaminyl (Gln)-tRNA synthetase. The isolated cDNA sequence corresponds to an internal section of a 5500 bases long mRNA that codes for a 170 kDa polypeptide associated with Gln-tRNA synthetase. Thus, the human enzyme is about three times larger than the E.coli and two times larger than the yeast Gln-tRNA synthetase. The three enzymes share an evolutionarily conserved core but differ in amino acid sequences linked to the N-terminal and C-terminal side of the core.


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