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.

Isolation of a Glyceraldehyde-3-Phosphate Dehydrogenase Gene from the Nematode, C. elegans

P.O. Yarbrough, M.A. Hayden, L.A. Dunn, P.S. Vermersch, M.R. Klass and R.M. Hecht

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.