Isolation of a cDNA encoding the B isozyme of human phosphoglycerate mutase (PGAM) and characterization of the PGAM gene family.
We previously reported the isolation of a full-length cDNA specifying the muscle-specific isozyme of human phosphoglycerate mutase (PGAM-M). We now report the isolation of a full-length cDNA specifying the non-muscle-specific, or brain (B), isozyme of human PGAM (PGAM-B). The PGAM-B cDNA encodes a deduced protein 254 amino acids long, 79% identical to PGAM-M, and contains a 913-nucleotide 3'-untranslated region, as compared to the unusually short 37-nucleotide 3'-untranslated region of PGAM-M. Northern analysis demonstrates the non-muscle-specific nature of PGAM-B transcription, while genomic Southern analysis implies the presence of a large PGAM family in the human genome. Most of the PGAM-hybridizing sequences in both the human and mouse genomes seem to be related to the B-isozyme gene; many members of the PGAM-B gene family in humans are apparently processed genes. These results agree with the evolutionary analysis, which indicates that the PGAM-B gene is the progenitor of the PGAM-M gene.
Sakoda
S
S
H. Houston Merritt Clinical Research Center for Muscular Dystrophy and Related Disorders, Columbia University College of Physicians and Surgeons, New York, New York 10032.
Shanske
S
S
DiMauro
S
S
Schon
E A
EA
D000595:Amino Acid Sequence; D001483:Base Sequence; D001731:Bisphosphoglycerate Mutase / Q000235:genetics*; D001921:Brain / Q000201:enzymology; D004247:DNA / Q000032:analysis*; D006801:Humans; D007527:Isoenzymes / Q000032:analysis / Q000235:genetics*; D008969:Molecular Sequence Data; D009132:Muscles / Q000201:enzymology; D010770:Phosphotransferases / Q000235:genetics*; D014176:Protein Biosynthesis; D014158:Transcription, Genetic
D007527:Isoenzymes; D004247:DNA; D010770:Phosphotransferases; D001731:Bisphosphoglycerate Mutase