Isolation of a cDNA encoding the B isozyme of human phosphoglycerate mutase (PGAM) and characterization of the PGAM gene family.
Isolation of a cDNA encoding the B isozyme of human phosphoglycerate mutase (PGAM) and characterization of the PGAM gene family.
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DOI:
10.1016/s0021-9258(18)37476-3
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发表时间:
1988-11
期刊:
影响因子:
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通讯作者:
S. Sakoda;S. Shanske;S. DiMauro;E. Schon
中科院分区:
文献类型:
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作者:
S. Sakoda;S. Shanske;S. DiMauro;E. Schon
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.