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Structure and organization of the human deoxyribonuclease II (DNase II) gene

Published online by Cambridge University Press:  01 July 1998

T. YASUDA
Affiliation:
Department of Legal Medicine, Gunma University School of Medicine, Gunma 371-8511, Japan
H. TAKESHITA
Affiliation:
Department of Legal Medicine, Gunma University School of Medicine, Gunma 371-8511, Japan
R. IIDA
Affiliation:
Department of Legal Medicine, Fukui Medical School, Fukui 910-1193, Japan
S. TSUTSUMI
Affiliation:
Department of Legal Medicine, Gunma University School of Medicine, Gunma 371-8511, Japan
T. NAKAJIMA
Affiliation:
Department of Legal Medicine, Gunma University School of Medicine, Gunma 371-8511, Japan
O. HOSOMI
Affiliation:
Department of Legal Medicine, Gunma University School of Medicine, Gunma 371-8511, Japan
Y. NAKASHIMA
Affiliation:
Department of Legal Medicine, Gunma University School of Medicine, Gunma 371-8511, Japan
S. MORI
Affiliation:
Department of Legal Medicine, Gunma University School of Medicine, Gunma 371-8511, Japan
K. KISHI
Affiliation:
Department of Legal Medicine, Gunma University School of Medicine, Gunma 371-8511, Japan
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Abstract

The structure of the human gene for deoxyribonuclease II (DNase II; EC 3.1.22.1) was determined using several specific primers based on the human DNase II cDNA sequence [Yasuda et al. (1998). J. Biol. Chem. 273, 2610–2616] in a polymerase chain reaction-based strategy. The gene spanned about 6 kb and consisted of 6 exons. No canonical TATA or CAAT boxes could be identified within the 1341 nucleotides upstream of the putative transcription start site, although the 5′-flanking region contained a CpG island and several putative binding motifs for transcription factors Sp1 and ETF. These properties indicate that the DNase II gene is a housekeeping gene and this is compatible with its ubiquitous expression in human tissues. Three different cleavage/polyadenylation sites were identified in the 3′-flanking region, leading to the production of multiple DNase II mRNA species. However, a comparison of the entire translated sequences of the gene from a pair of subjects with homozygous DNase II phenotypes H and L revealed no differences in the nucleotide sequences.

Type
Research Article
Copyright
© University College London 1998

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