Nucleic Acids Research, Vol 25, Issue 4 750-755, Copyright © 1997 by Oxford University Press
H Nilsen, M Otterlei, T Haug, K Solum, TA Nagelhus, F Skorpen and HE Krokan
A distinct nuclear form of human uracil-DNA glycosylase [UNG2, open reading
frame (ORF) 313 amino acid residues] from the UNG gene has been identified.
UNG2 differs from the previously known form (UNG1, ORF 304 amino acid
residues) in the 44 amino acids of the N-terminal sequence, which is not
necessary for catalytic activity. The rest of the sequence and the
catalytic domain, altogether 269 amino acids, are identical. The
alternative N-terminal sequence in UNG2 arises by splicing of a previously
unrecognized exon (exon 1A) into a consensus splice site after codon 35 in
exon 1B (previously designated exon 1). The UNG1 sequence starts at codon 1
in exon 1B and thus has 35 amino acids not present in UNG2. Coupled
transcription/translation in rabbit reticulocyte lysates demonstrated that
both proteins are catalytically active. Similar forms of UNG1 and UNG2 are
expressed in mouse which has an identical organization of the homologous
gene. Constructs that express fusion products of UNG1 or UNG2 and green
fluorescent protein (EGFP) were used to study the significance of the
N-terminal sequences in UNG1 and UNG2 for subcellular targeting. After
transient transfection of HeLa cells, the pUNG1-EGFP-N1 product colocalizes
with mitochondria, whereas the pUNG2-EGFP-N1 product is targeted
exclusively to nuclei.
ARTICLES
Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene
UNIGEN Center for Molecular Biology, Medical Faculty, Norwegian University of Science and Technology, Trondheim.
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