The JMJD2 members of histone demethylase revisited.
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.
Division of Biotechnology, Dalian Institute of Chemical Physics, CAS, 457 Zhongshan Road, Dalian, 116023, PR China. hdt@dicp.ac.cn
Haidong
H
Tan
Siguo
S
Wu
Jinxia
J
Wang
Zongbao Kent
ZK
Zhao
D000595:Amino Acid Sequence; D006657:Histones / Q000378:metabolism*; D008239:Lysine / Q000235:genetics / Q000378:metabolism; D008745:Methylation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010089:Oxidoreductases, N-Demethylating / Q000378:metabolism*; D011487:Protein Conformation
D006657:Histones; D010089:Oxidoreductases, N-Demethylating; D008239:Lysine