Structural Organization of the Mouse DNA Repair Gene, N-Methylpurine-DNA Glycosylase

Masaaki Tatsuka, Gordon C. Ibeanu, Tadahide Izumi, Satya Narayan, C. V. Ramana, Nam Keun Kim, Wenli Kang, Gargi Roy, Sankar Mitra

Research output: Contribution to journalArticlepeer-review

21 Scopus citations


N-Methylpurine-DNA glycosylase (MPG), a ubiquitous DNA repair enzyme, removes N-alkylpurines and other purine lesions induced in DNA by simple alkylating carcinogens. A mouse MPG cDNA clone was isolated from a λ recombinant phage library of BALB/c mouse lung cell and characterized. Using the mouse MPG cDNA as a probe, the complete mouse MPG gene was isolated in two overlapping λ recombinant genomic clones. The 6-kb gene has four exons containing 1,002 bp of coding sequence. The transcription start site was identified in the genomic sequence by primer extension of MPG mRNA from a mouse lung fibroblast cell line. The location of this transcription start site was confirmed by in vitro transcription with the promoter-containing plasmid template. Promoter function of the sequence 5' upstream of the transcription initiation site was shown by transient expression of the firefly luciferase reporter gene under the control of this sequence in transfected human and mouse cells. The mouse MPG promoter contains no TATA box, but has a CAAT element and is G·C-rich with putative AP2 elements and SP1-complementary sequences.

Original languageEnglish
Pages (from-to)37-45
Number of pages9
JournalDNA and Cell Biology
Issue number1
StatePublished - Jan 1995

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology


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