Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity and molecular evolution of the gene

TLDR

Full-length cDNAs encoding the glycolytic enzyme GAPDH have been identified in rat and human genomes by genomic blot hybridization, yet only a single functional gene product has been reported. The study compares rat and human GAPDH cDNA sequences with those from chicken, Drosophila, and yeast to analyze the gene’s evolutionary history. Genomic library screening uncovered 300–400 GAPDH-related sequences in the rat genome and about 100 in the human genome, many of which are transcribed pseudogenes, and rat and human cDNAs share 89 % coding‑region homology and 76 % homology in the first 100 bp of the 3′ noncoding region.

Abstract

Full length cDns encoding the glycolyti enzme glyceraldehyde-3-phosphate dehyrogense (GAPDH)fron rat man have been in both genomes based on genmic blot hybridization analysis. Only one functional gene product is know. Result fron genomic library screeings suggest that are 300–400 copies of these sequences in the rat genome and approximately 100 in the human genome, Some of these realted sequences have been shown to be thesepseudogenes indicating that some pseudogenes are transcrined. Rat and human cDNA are 89% homologous in the coding region, and 76% homologous in the frist 100 base paris of the 3' -noncoding region. Comparison of these two cDNA sequences with those of the chicken, Drosophils and yeast genes allows analysis of the evolution of the GAPDH genes in detail.