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

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (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), Vol. 88:19; ISSN 0027-8424
Country of Publication:
United States
Language:
English