Disease relevance of gpd-2

• We found that not only is the daf-2(e1370)-enhanced anoxia phenotype dependent upon gpd-2 and gpd-3, but also the motility of animals exposed to brief periods of anoxia is prematurely arrested in gpd-2/3(RNAi) and daf-2(e1370);gpd-2/3(RNAi) animals [1].

High impact information on gpd-2

• Previous studies have indicated a relationship between these two events in the processing of a heat shock-induced gpd-2-gpd-3 polycistronic pre-mRNA [2].
• Changing the AGUAAA to AAUAAA also influenced the trans-splicing process: with AGUAAA, most of the gpd-2 product was trans-spliced to SL1, rather than SL2, which is normally used at downstream operon trans-splice sites [3].
• However, with AAUAAA, SL2 trans-splicing of gpd-2 was increased [3].
• Finally, an open reading frame found several hundred nucleotides upstream from gpd-2, in both species, appears to be homologous to the ATP synthase subunit, ATPase inhibitor protein, from bovine mitochondria [4].

Biological context of gpd-2

• We identified gpd-2 and gpd-3, two nearly identical genes in an operon that encode the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase [1].
• The direct tandem organization of these genes, gpd-2 and gpd-3, and the size and location of the two introns in each gene are the same in C. elegans and C. briggsae [4].

Analytical, diagnostic and therapeutic context of gpd-2

• As defined by starch gel electrophoresis, the faster-migrating isoenzyme, glyceraldehyde-3-phosphate dehydrogenase-2, increases its activity during postembryonic development [5].

References