Worm Breeder's Gazette 9(2): 19
These abstracts should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.
The isolation and genomic sequence of one of possibly four glyceraldehyde-3-phosphate dehydrogenase (GAPDH) genes in the nematode, Caenorhabditis nted. The complete nucleotide sequence of the coding as well as the noncoding flanking regions of this gene has been determined (see figure). The deduced amino acid sequence agrees with the sequence of typical glyceraldehyde- 3-phosphate dehydrogenase enzymes and its molecular weight of 36,235 daltons agrees with its size determined previously (P. Yarbrough and R. Hecht, J. Biol. Chem. 259:14711-14720). That this isolated gene encodes a nematode GAPDH is additionally confirmed by demonstrating its immunoreactivity to an anti-nematode GAPDH antibody after its expression as a fused protein with dihydrofolate reductase. Codon utilization follows a pattern typical of other expressed nematode genes. The gene is split by two introns that are highly conserved in comparison to other introns observed in C. elegans. The placement of one of these introns is conserved with respect to the chicken GAPDH gene. Within the 5' flanking sequence homology to actin and the homology 2 block of the major myosin gene (unc-54) is noted. Preliminary results suggest that this GAPDH gene encodes a minor isoenzyme of C. elegans. It is of interest that the 3' flanking region contains a CAAAT box, followed by a TATAAT box before an open reading frame of a closely linked gene that also contains a small AT rich intron with the nematode consensus splice junction.