A mammalian apurinic/apyrimidinic endonuclease (AP endonuclease) is known to have two distinct functional domains. One domain is responsible for regulating the activity of Fos/Jun proto-oncogene products to bind to DNA at specific recognition sites. The other domain which is highly conserved from bacteria to mammals, is responsible for repairing DNA damage caused by ionizing radiation, oxidative damage, and alkylating agents. This study reports on the isolation and characterization of the genomic structure of the mouse AP endonuclease gene (Apex). The genomic sequence of the Apex gene was 2.14 kb in length and contained four exons. Exon 1 contained a 0.24-kb untranslated 5′ region upstream of the initiation codon. Consensus sequences for two CAAT boxes and a GC box were found upstream of the end of exon 1. A polymorphism was noted in the untranslated region of exon 1 in a comparison of a number of mouse strains. These data indicate that the 5′ end of the mouse gene (Apex) differs from the previously isolated human gene (Ape), which has five exons and an untranslated region between exons 1 and 2. Data are also presented that suggest the presence of two pseudogenes in the mouse.
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Breathnach, R., Chambon, P. (1981). Organization and expression of eucaryotic split genes coding for proteins. Annu. Rev. Biochem. 50, 349–383.
Cheng, X., Bunville, J., Patterson, T.A. (1992). Nucleotide sequence of a cDNA for an apurinic/apyrimidinic endonuclease from HeLa cells. Nucleic Acids. Res. 20, 370.
Cunningham, R.P., Saporito, S.M., Spitzer, S.G., Weiss, B. (1986). Endonuclease IV (nfo) mutant of Escherichia coli. J. Bacteriol. 168, 1120–1127.
Demple, B., Herman, T., Chen, D.S. (1991). Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes. Proc. Natl. Acad. Sci. USA 88, 11450–11454.
Doetsch, P.W., Cunningham, R.P. (1990). The enzymology of apurinic/apyrimininic endonucleases. Mutation Res. 236, 173–201.
Harrison, L., Ascione, G., Menninger, J.C., Ward, D.C., Demple, B. (1992). Human apurinic endonuclease gene (APE): structure and genomic mapping (chromosome 14q11.2-12). Hum. Mol. Genet. 1, 677–680.
Kerppola, T.K., Curran, T. (1991). Transcription factor interactions: basics on zippers. Curr. Opin. Struct. Biol. 1, 71–79.
Morgan, J.I., Curran, T. (1991). Stimulus-transcription coupling in the nervous system: involvement of the inducible proto-oncogenes fos and jun. Annu. Rev. Neurosci, 14, 421–451.
Mudgett, J.S., MacInnes, M.A. (1990). Isolation of the functional excision repair gene ERCC5 by intercosmid recombination. Genomics 8, 623–633.
Padgett, R.A., Grabowski, P.J., Konarska, M.M., Seiler, S., Sharp, P.A. (1986). Splicing of messenger RNA precursors. Annu. Rev. Biochem. 55, 1119–1150.
Robson, C.N., Hickson, I.D. (1991). Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants. Nucleic Acids Res. 20, 5519–5523.
Robson, C.N., Milne, A.M., Pappin, D.J.C., Hickson, I.D. (1991). Isolation of cDNA clones encoding an enzyme from bovine cells that repair oxidative DNA damage in vitro: homology with bacterial repair enzymes. Nucleic Acids Res. 19, 1087–1092.
Robson, C.N., Hochhauser, D., Craig, R., Rack, K., Buckle, V.J., Hickson, I.D. (1992). Structure of the human DNA repair gene Hap 1 and its localisation to chromosome 14q 11.2–12. Nucleic Acids Res. 20, 4417–4421.
Saporito, S.M., Smith-White, B.J., Cunningham, R.P. (1988). Nucleotide sequence of the xth gene of Escherichia coli K-12. J. Bacteriol. 170, 4542–4547.
Seki, S., Akiyama, K., Watanabe, S., Hatsushika, M., Ikeda, S., Tsutsui, K. (1991). cDNA and deduced amino acid sequence of a mouse DNA repair enzyme (APEX nuclease) with significant homology to Escherichia coli exonuclease III. J. Biol. Chem. 266, 20797–20802.
Seki, S., Hatsushika, M., Watanabe, S., Akiyama, K., Nagao, K., Tsutsui, K. (1992). cDNA cloning, sequencing, expression and possible domain structure of human APEX nuclease homologous to Escherichia coli exonuclease III. Biochim. Biophys. Acta 1131, 287–299.
Walker, L.J., Robson, C.N., Black, E., Gillespie, D., Hickson, I.D. (1993). Identification of residues in the human DNA repair enzyme HAP 1 (Ref-1) that are essential for redox regulation of Jun DNA binding. Mol. Cell. Biol. 13, 5370–5376.
Xanthoudakis, S., Curran, T. (1992). Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity. EMBO J. 11, 653–665.
Xanthoudakis, S., Miao, G., Wang, F., Pan, Y.E., Curran, T. (1992). Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J. 11, 3323–3335.
Zhao, B., Grandy, D.K., Hagerup, J.M., Magenis, R.E., Smith, L., Chauhan, B.C., Henner, W.D. (1992). The human gene for apurinic/apyrimidinic endonuclease (HAP 1): sequence and localization to chromosome 14 band q12. Nucleic Acids Res. 20, 4097–4098.
The nucleotide sequence data reported in this paper has been submitted to the GeneBank data library, and the accession number is U12273.
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Takiguchi, Y., Chen, D.J. Genomic structure of the mouse apurinic/apyrimidinic endonuclease gene. Mammalian Genome 5, 717–722 (1994). https://doi.org/10.1007/BF00426079
- Consensus Sequence
- Untranslated Region
- Mouse Strain
- Recognition Site