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Nucleic Acids Research, 1995, Vol. 23, No. 8 1307-1310
© 1995

MOLECULAR BIOLOGY

Cloning, sequencing and bacterial expression of human glycine tRNA synthetase

James Williams*, Sarah Osvath, Tee Fern Khong, Martin Pearse and David Power

Immunology Research Centre, St Vincents Hospital 41 Victoria Parade, Fitzroy, Victoria 3065, Australia

* To whom correspondence should be addressed at present address: Department of Biochemistry. Royal Perth Hospital. GPO Box X2213. Perth. WA 6001. Australia

Received January 19, 1995. Revised March 13, 1995. Accepted March 13, 1995.

ABTRACT: The human glycine tRNA synthetase gene (GlyRS) has been cloned and sequenced. The 2462 bp cDNA for this gene contains alarge open reading frame (ORF) encoding 685 amino acids with predicted Mr=77 507 Da. The protein sequence has ~60% identity with B.moriGlyRS and 45% identity with S.cerevisiaeGlyRS and contains motifs 2 and 3 characteristic of Class II tRNA synthetases. A second ORF encoding 47 amino acids isfound upstream of the large ORF. Translation of this ORF may precede the expression of GlyRS as a possible regulatory mechanism. The enzyme was expressed in E.coli as a fusion protein with a 13 kDa biotinylated tag with an apparent Mr = 90 kDa. The fusion protein was immunoprecipitated from crude bacterial extract with human EJ serum, which contains autoantibodies directed against GlyRS, and with rabbit polyclonal serum raised against a synthetic peptide derived from the predicted amino acid sequence of human GlyRS. Bacterial extract containing the fusion protein catalyses the aminoacylation of bovine tRNA with [14C]-gly at 10-fold increased level above normal bacterial extractand confirms that the cDNA encodes human GlyRS.


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