A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase

Journal Article · Tue Oct 01 04:00:00 EDT 1991 · Proceedings of the National Academy of Sciences of the United States of America; (United States)

DOI:https://doi.org/10.1073/pnas.88.19.8460· OSTI ID:5703507

Meyer-Siegler, K; Mauro, D J; Seal, G; Wurzer, J; DeRiel, J K; Sirover, M A ^[1]

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1. Temple Univ., Philadelphia, PA (United States)

The authors have isolated and characterized a plasmid (pChug 20.1) that contains the cDNA of a nuclear uracil DNA glycosylase (UDG) gene isolated from normal human placenta. This cDNA directed the synthesis of a fusion protein that exhibited UDG activity. The enzymatic activity was specific for a uracil-containing polynucleotide substrate and was inhibited by a glycosylase antibody or a {beta}-galactosidase antibody. Sequence analysis demonstrated an open reading frame that encoded a protein of 335 amino acids of calculated M{sub r} 36,050 and pI 8.7, corresponding to the M{sub r} 37,000 and pI 8.1 of purified human placental UDG. Surprisingly, a search of the GenBank data base revealed that the cDNA of UDG was completely homologous with the 378-kDa subunit of human glyceraldehyde-3-phosphate dehydrogenase. Human erythrocyte glyceraldehyde-3-phosphate dehydrogenase was obtained commercially in its tetrameric form. A 37-kDa subunit was isolated form it and shown to possess UDG activity equivalent to that seen for the purified human placental UDG. The multiple functions of this 37-kDa protein as here and previously reported indicate that it possesses a series of activities, depending on its oligomeric state. Accordingly, mutation(s) in the gene of this multifunctional protein may conceivably result in the diverse cellular phenotypes of Bloom syndrome.

• OSTI ID: 5703507
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (United States), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (United States) Vol. 88:19; ISSN 0027-8424; ISSN PNASA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
AZINES
BACTERIA
BIOLOGICAL MATERIALS
BIOLOGICAL RECOVERY
BIOLOGICAL REPAIR
BLOOD
BLOOD CELLS
BODY FLUIDS
DISEASES
DNA
DNA REPAIR
DNA SEQUENCING
ELECTROPHORESIS
ENZYME ACTIVITY
ENZYMES
ERYTHROCYTES
ESCHERICHIA COLI
ETIOLOGY
GENE MUTATIONS
GENES
GLYCOSYL HYDROLASES
HEREDITARY DISEASES
HETEROCYCLIC COMPOUNDS
HYDROGEN COMPOUNDS
HYDROLASES
HYDROXY COMPOUNDS
MATERIALS
MICROORGANISMS
MUTATIONS
NUCLEIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PHENOTYPE
PROTEINS
PYRIMIDINES
RECOMBINANT DNA
RECOVERY
REPAIR
STRUCTURAL CHEMICAL ANALYSIS
SUBSTRATES
TRITIUM COMPOUNDS
URACILS