Worm Breeder's Gazette 10(2): 36

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.

Colocalization of Nematode Myofilaments and mRNAs for GAPDH and Actin

Xinyun Huang and Ralph Hecht

Glyceraldehyde-3-phosphate dehydrogenase is encoded by four genes in 
the nematode C.  elegans.  The minor isoenzyme, GAPDH-1, is encoded by 
two nearly identical genes namely gpd-1 and gpd-4.  In agreement with 
the ontogeny of GAPDH-1 enzyme activity, both mRNAs were 
preferentially expressed in embryos which are predominantly composed 
of non-muscle cells GAPDH-2, a body-wall enriched isoenzyme, is 
encoded by a different set of nearly identical genes, gpd-2 and gpd-3. 
Their expression increases 10-fold during post-embryonic development. 
Furthermore, the mRNAs of gpd-2 and gpd-3 were exclusively observed 
in the body-wall muscle by in situ hybridization.  By minimizing 
diffusion during hybridization, the gpd-2,3 mRNAs were localized to 
the actin-containing zones as was the GAPDH-2 isoenzyme itself.  By in 
situ hybridization we further demonstrated that the actin genes act-1 
and act-3 encoded body-wall specific mRNAs that were also localized to 
the thin myofilaments.