NEIL1 mRNA Splicing Variants are Expressed in Normal Mouse Organs

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  • YAMAMOTO Ryohei
    Department of Advanced Pathobiology, Graduate School of Life & Environmental Sciences, Osaka Prefecture University
  • YAMAMOTO Mizuki
    Department of Advanced Pathobiology, Graduate School of Life & Environmental Sciences, Osaka Prefecture University
  • KUSAKA Hiroyuki
    Department of Advanced Pathobiology, Graduate School of Life & Environmental Sciences, Osaka Prefecture University
  • MASATSUGU Hideaki
    Department of Advanced Pathobiology, Graduate School of Life & Environmental Sciences, Osaka Prefecture University
  • MATSUYAMA Satoshi
    Department of Advanced Pathobiology, Graduate School of Life & Environmental Sciences, Osaka Prefecture University
  • TAJIMA Tomoko
    Department of Infectious Diseases Control, Graduate School of Life & Environmental Sciences, Osaka Prefecture University
  • IDE Hiroshi
    Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University
  • KUBO Kihei
    Department of Advanced Pathobiology, Graduate School of Life & Environmental Sciences, Osaka Prefecture University

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Oxidized pyrimidines are mainly repaired by base excision repair, which is initiated by damage-specific DNA glycosylases. NEIL1, the mammalian homolog of Escherichia coli endonuclease VIII and a major DNA glycosylase, initiates repair of oxidized pyrimidines. Here, we investigated the expression of two putative variant mouse NEIL1 (mNEIL1) mRNAs—variant 1 ("Neil1 protein" mRNA; BC043297 in the NCBI database) and variant 2 ("unnamed protein" mRNA; AK040802 in the NCBI database)—in normal mouse organs. Reverse transcription-PCR showed that both mRNAs were expressed in total RNA samples from 9 organs. Immunoblot analysis of a nuclear extract from normal mouse liver revealed three bands corresponding to full-length mNEIL1 protein and the two predicted variant proteins. However, neither variant protein, which included an N-terminal enzymatic activity domain deduced from the mRNA variants, were enzymatically active under multiple reaction conditions when expressed as his-tagged recombinant proteins. Nevertheless, recombinant variant 1 protein influenced mNEIL1 activity, while recombinant variant 2 protein had no influence. These results suggest that mNEIL1 mRNA variants are expressed in a variety of organs in normal mice and that variant 1 protein may regulate mNEIL1 activity.

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