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Phosphoglucomutase: Structural studies of the PGM1 gene and a search for PGM3 and PGM4

Ives, Jane Hilda; (1995) Phosphoglucomutase: Structural studies of the PGM1 gene and a search for PGM3 and PGM4. Doctoral thesis (Ph.D), UCL (University College London). Green open access

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Phosphoglucomutase is an enzyme central to glycolysis and gluconeogenesis. There are three well characterised forms: PGM1, PGM2 and PGM3. Genomic clones containing the 5' end of the PGM1 gene were isolated and characterised. The exon/intron boundaries of the first exon (designated 1 A) were determined. 15kb of intron 1 have been mapped and 2.8kb of the flanking regions sequenced. The proximal promoter shows features of a 'housekeeping' promoter. Features characteristic of a CpG island have been identified in this region. An alternative first exon has been identified (1B). The two exons show similarities indicating a gene duplication event. Exon 1B is transcribed from a promoter in the first large intron of PGM 1.1 A. Expression studies of PGM 1.IB by RNA-PCR show a limited tissue expression, with predominate expression in striated muscle. Exons 1A and 1B were sequenced in DNA from eight individuals of known PGM1 protein phenotypes. No genetic variation in these sequences was encountered. The PGM1 cDNA was used as a probe in a search for the PGM3 gene. A human chromosome 6 library was screened. Positive cosmids were assigned to chromosome positions by fluorescent in situ hybridisation, restriction mapped and sequenced in part. These studies led to the identification of a novel PGM on chromosome 9. PGM3 was not isolated by this procedure, suggesting that the sequences of PGM1 and PGM3have diverged significantly. Mammary gland cDNA libraries were screened using both anti-PGM1 antibodies and PGM1 cDNA, to search for PGM4. Positive clones were all identified as PGM1. In addition the PGM1 type of DNA from recent mothers was compared to the typing of matched colostrum samples (by isoelectric focusing). Some similarities were seen between the colostrum and PGM1 isoform patterns. Together, these data suggest that PGM4 protein is a modified form of PGM1.

Type: Thesis (Doctoral)
Qualification: Ph.D
Title: Phosphoglucomutase: Structural studies of the PGM1 gene and a search for PGM3 and PGM4
Open access status: An open access version is available from UCL Discovery
Language: English
Additional information: Thesis digitised by ProQuest.
URI: https://discovery.ucl.ac.uk/id/eprint/10103485
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