The functional impact of Pgm amino acid polymorphism on glycogen content in Drosophila melanogaster.

Earlier studies of the common PGM allozymes in Drosophila melanogaster reported no in vitro activity differences. However, our study of nucleotide variation observed that PGM allozymes are a heterogeneous mixture of amino acid polymorphisms. In this study, we analyze 10 PGM protein haplotypes with respect to PGM activity, thermostability, and adult glycogen content. We find a twofold difference in activity among PGM protein haplotypes that is associated with a threefold difference in glycogen content. The latitudinal clines for several Pgm amino acid polymorphisms show that high PGM activity, and apparently higher flux to glycogen synthesis, parallel the low activity clines at G6PD for reduced pentose shunt flux in northern latitudes. This suggests that amino acid polymorphism is under selection at this branch point and may be favored for increased metabolic storage associated with stress resistance and adaptation to temperate regions.