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Histochemistry and Cell Biology

, Volume 143, Issue 3, pp 259–266 | Cite as

Coordinated expression of H3K9 histone methyltransferases during tooth development in mice

  • Taichi Kamiunten
  • Hisashi Ideno
  • Akemi Shimada
  • Yoshiki Nakamura
  • Hiroshi Kimura
  • Kazuhisa Nakashima
  • Akira NifujiEmail author
Original Paper

Abstract

Tissue-specific gene expression is subjected to epigenetic and genetic regulation. Posttranslational modifications of histone tails alter the accessibility of nuclear proteins to DNA, thus affecting the activity of the regulatory complex of nuclear proteins. Methylation at histone 3 lysine 9 (H3K9) is a crucial modification that affects gene expression and cell differentiation. H3K9 is known to have 0–3 methylation states, and these four methylated states are determined by the expression of sets of histone methyltransferases. During development, teeth are formed through mutual interactions between the mesenchyme and epithelium via a process that is subjected to the epigenetic regulation. In this study, we examined the expression of all H3K9 methyltransferases (H3K9MTases) during mouse tooth development. We found that four H3K9MTases—G9a, Glp, Prdm2, and Suv39h1—were highly expressed in the tooth germ, with expression peaks at around embryonic days 16.5 and 17.5 in mice. Immunohistochemical and in situ hybridization analyses revealed that all four H3K9MTases were enriched in the mesenchyme more than in the epithelium. Substrates of H3K9MTases, H3K9me1, H3K9me2, and H3K9me3 were also enriched in the mesenchyme. Taken together, these data suggested that coordinated expression of four H3K9MTases in the dental mesenchyme might play important roles in tooth development.

Keywords

Histone methylation Tooth development Cell differentiation Gene expression 

Abbreviations

H3K9me1

Monomethylated lysine 9 at histone H3

H3K9me2

Dimethylated lysine 9 at histone H3

H3K9me3

Trimethylated lysine 9 at histone H3

H3K9MTase

H3K9 methyltransferase

Notes

Acknowledgments

This study was supported by grants-in-aid funding for scientific research (JSPS KAKENHI Grant Numbers 22390344, 23659862, 25670784 to A.N.).

Conflict of interest

There is no conflict of interest.

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Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  • Taichi Kamiunten
    • 1
    • 2
  • Hisashi Ideno
    • 1
    • 3
  • Akemi Shimada
    • 1
  • Yoshiki Nakamura
    • 2
  • Hiroshi Kimura
    • 4
  • Kazuhisa Nakashima
    • 1
  • Akira Nifuji
    • 1
    • 3
    Email author
  1. 1.Department of PharmacologyTsurumi University School of Dental MedicineYokohamaJapan
  2. 2.Department of OrthodonticsTsurumi University School of Dental MedicineYokohamaJapan
  3. 3.Transcriptome Research GroupNational Institute of Radiological SciencesChibaJapan
  4. 4.Graduate School of Bioscience and BiotechnologyTokyo Institute of TechnologyYokohamaJapan

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