Analysis of the cDNA and encoded protein of the human testis-specific PGK-2 gene.

Because of their unique function, germ cells require unique gene products. Thus, although the glycolytic enzyme phosphoglycerate kinase (PGK) is required in all metabolically active cell types, there are two functional PGK genes in the mammalian genome, one, PGK-1, that is X-linked and ubiquitously expressed in all somatic tissues, and a second, PGK-2, that is autosomal and expressed only in spermatogenic cells. Expression of the PGK-2 gene may function solely to compensate for repressed expression of the PGK-1 gene due to X-chromosome inactivation in spermatocytes. Alternative y, the PGK-2 gene could encode an isozyme with unique characteristics that are beneficial to spermatozoa. We have isolated a cDNA of the human PGK-2 gene and used this as probe to demonstrate that transcription of this gene in spermatocytes and spermatids coincides with a period of repressed transcription of the X-linked PGK-1 gene during spermatogenesis in the human testis. We have also analyzed the amino acid sequence and protein characteristics of the PGK-2 isozyme deduced from this cDNA and compared them with that of the human PGK-1 isozyme to show that known structural and functional motifs are conserved in both proteins. Finally, we have examined the distribution of the PGK-1 and PGK-2 isozymes during spermatogenesis in the mouse to show that while the PGK-2 protein does not appear to possess any unique intracellular localization signal, it is more stable in vivo than the PGK-1 protein.