Molecular analysis of the human and marsupial PGP9.5 gene
Molecular analysis of the human and marsupial PGP9.5 gene
Protein Gene Product (PGP) 9.5 was first described in human brain where it makes up 1-2% of total brain soluble protein. Immunohistochemistry showed PGP9.5 to be widely distributed in central and peripheral neurones and in cells of the diffuse neuroendocrine system. The structure of the human PGP9.5 protein was deduced from the sequence of a cDNA clone and was subsequently found to show a high level of homology with a ubiquitin C-terminal hydrolase (UCH) isoenzyme. Purified PGP9.5 protein has been shown to have UCH activity and is now known to be a neurone-specific member of a family of UCH isoenzymes, designated UCH-L1.
Little is known about the factors which control neurone-specific gene expression. Since PGP9.5 is an abundant neurone-specific protein, its structural gene is an ideal model for studies on the transcription of neurone specific genes. The structure of the human gene encoding PGP9.5 was already known, but an animal model, Monodelphis domestica, the grey short-tailed opossum, was used for further studies on the cDNA and structural gene for PGP9.5. The results from the cDNA sequencing show PGP9.5 to be a highly conserved protein, with considerable homology to other members of the UCH isoenzyme family, but the potential isoprenylation site at the C-terminus of PGP9.5 is not found in the other isoenzymes.
The construction of a Monodelphis genomic library provides a valuable resource for future studies on Monodelphis genes. The molecular analysis of the PGP9.5 gene shows it to have an identical exon structure (at least for the first three exons) to the human gene. Further sequencing of a newly isolated human PGP9.5 genomic clone was carried out and comparison of the 5' upstream regions from this and the Monodelphis gene allowed the identification of several potential regulatory sequences in this portion of the gene. These sequences may be involved in the control of PGP9.5 gene expression and possibly have a wider role in the regulation of transcription in neurone-specific genes.
University of Southampton
1993
Lavender, Frances Louise
(1993)
Molecular analysis of the human and marsupial PGP9.5 gene.
University of Southampton, Doctoral Thesis.
Record type:
Thesis
(Doctoral)
Abstract
Protein Gene Product (PGP) 9.5 was first described in human brain where it makes up 1-2% of total brain soluble protein. Immunohistochemistry showed PGP9.5 to be widely distributed in central and peripheral neurones and in cells of the diffuse neuroendocrine system. The structure of the human PGP9.5 protein was deduced from the sequence of a cDNA clone and was subsequently found to show a high level of homology with a ubiquitin C-terminal hydrolase (UCH) isoenzyme. Purified PGP9.5 protein has been shown to have UCH activity and is now known to be a neurone-specific member of a family of UCH isoenzymes, designated UCH-L1.
Little is known about the factors which control neurone-specific gene expression. Since PGP9.5 is an abundant neurone-specific protein, its structural gene is an ideal model for studies on the transcription of neurone specific genes. The structure of the human gene encoding PGP9.5 was already known, but an animal model, Monodelphis domestica, the grey short-tailed opossum, was used for further studies on the cDNA and structural gene for PGP9.5. The results from the cDNA sequencing show PGP9.5 to be a highly conserved protein, with considerable homology to other members of the UCH isoenzyme family, but the potential isoprenylation site at the C-terminus of PGP9.5 is not found in the other isoenzymes.
The construction of a Monodelphis genomic library provides a valuable resource for future studies on Monodelphis genes. The molecular analysis of the PGP9.5 gene shows it to have an identical exon structure (at least for the first three exons) to the human gene. Further sequencing of a newly isolated human PGP9.5 genomic clone was carried out and comparison of the 5' upstream regions from this and the Monodelphis gene allowed the identification of several potential regulatory sequences in this portion of the gene. These sequences may be involved in the control of PGP9.5 gene expression and possibly have a wider role in the regulation of transcription in neurone-specific genes.
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Published date: 1993
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Local EPrints ID: 462216
URI: http://eprints.soton.ac.uk/id/eprint/462216
PURE UUID: cc06a450-2631-4a5f-b4d8-8ad7495a1e41
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Date deposited: 04 Jul 2022 19:04
Last modified: 04 Jul 2022 19:04
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Author:
Frances Louise Lavender
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