Histone-lysine N-methyltransferase SETMAR
Definition:
References:
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[1]. R Hromas, et al. Chk1 phosphorylation of Metnase enhances DNA repair but inhibits replication fork restart. Oncogene. 2012 Sep 20;31(38):4245-54. [Content Brief]
[2]. Leyma P De Haro, et al. Metnase promotes restart and repair of stalled and collapsed replication forks. Nucleic Acids Res. 2010 Sep;38(17):5681-91. [Content Brief]
[3]. Sheema Fnu, et al. Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining. Proc Natl Acad Sci U S A. 2011 Jan 11;108(2):540-5. [Content Brief]
[4]. Brian D Beck, et al. Human Pso4 is a metnase (SETMAR)-binding partner that regulates metnase function in DNA repair. J Biol Chem. 2008 Apr 4;283(14):9023-30. [Content Brief]
[5]. Kristie D Goodwin, et al. Crystal structure of the human Hsmar1-derived transposase domain in the DNA repair enzyme Metnase. Biochemistry. 2010 Jul 13;49(27):5705-13. [Content Brief]
[6]. Richard Cordaux, et al. Birth of a chimeric primate gene by capture of the transposase gene from a mobile element. Proc Natl Acad Sci U S A. 2006 May 23;103(21):8101-6. [Content Brief]
[7]. Elizabeth A Williamson, et al. The SET and transposase domain protein Metnase enhances chromosome decatenation: regulation by automethylation. Nucleic Acids Res. 2008 Oct;36(18):5822-31. [Content Brief]
[8]. Yaritzabel Roman, et al. Biochemical characterization of a SET and transposase fusion protein, Metnase: its DNA binding and DNA cleavage activity. Biochemistry. 2007 Oct 9;46(40):11369-76. [Content Brief]
[9]. Hyun-Suk Kim, et al. The DDN catalytic motif is required for Metnase functions in non-homologous end joining (NHEJ) repair and replication restart. J Biol Chem. 2014 Apr 11;289(15):10930-10938. [Content Brief]
[10]. Suk-Hee Lee, et al. The SET domain protein Metnase mediates foreign DNA integration and links integration to nonhomologous end-joining repair. Proc Natl Acad Sci U S A. 2005 Dec 13;102(50):18075-80. [Content Brief]
[11]. Csaba Miskey, et al. The ancient mariner sails again: transposition of the human Hsmar1 element by a reconstructed transposase and activities of the SETMAR protein on transposon ends. Mol Cell Biol. 2007 Jun;27(12):4589-600. [Content Brief]