Molecular Biology Reports

, Volume 35, Issue 4, pp 551–556 | Cite as

The JMJD2 members of histone demethylase revisited

  • Haidong Tan
  • Siguo Wu
  • Jinxia Wang
  • Zongbao (Kent) Zhao


The study of histone lysine demethylases has become very hot recently. Many histone demethylases have been reported by different research groups with various techniques. However, how many histone lysine-methylation states can be removed by one specific demethylase and how many demethylases can remove one specific histone lysine-methylation state? It remains a daunting challenge to answer these questions to date. An in-depth discussion on recent results, three important points were provided: (1) Some demethylases can remove more histone lysine-methylation states; (2) Some prokaryotes might be endowed with histone lysine demethylases although they are devoid of histones; (3) Protein-protein interaction provides a valuable framework for a better understanding of the functions of the histone lysine demethylases. All of these will be beneficial to a better understanding of demethylases and suggest how future research can be improved.


Eukaryotes Histone demethylation In vivo study JMJD2 Prokaryotes Protein-protein interaction 



This work was supported by CAS “100 Talents” program. The authors also thank the anonymous reviewers for a number of suggestions that have improved the quality of the paper.


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Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  • Haidong Tan
    • 1
  • Siguo Wu
    • 1
  • Jinxia Wang
    • 1
  • Zongbao (Kent) Zhao
    • 1
  1. 1.Division of BiotechnologyDalian Institute of Chemical Physics, CASDalianP.R. China

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