Preprint Review Version 1 Preserved in Portico This version is not peer-reviewed

Structure, Activity, and Function of SETMAR protein Lysine Methyltransferase

Version 1 : Received: 5 November 2021 / Approved: 9 November 2021 / Online: 9 November 2021 (11:30:21 CET)

A peer-reviewed article of this Preprint also exists.

Tellier, M. Structure, Activity, and Function of SETMAR Protein Lysine Methyltransferase. Life 2021, 11, 1342. Tellier, M. Structure, Activity, and Function of SETMAR Protein Lysine Methyltransferase. Life 2021, 11, 1342.


SETMAR is a protein lysine methyltransferase that is involved in several DNA processes, including DNA repair via the non-homologous end joining (NHEJ) pathway, regulation of gene expression, illegitimate DNA integration, and DNA decatenation. However, SETMAR is an atypical protein lysine methyltransferase since in anthropoid primates, the SET domain is fused to an inactive DNA transposase. The presence of the DNA transposase domain confers to SETMAR a DNA binding activity towards the remnants of its transposable element, which has resulted in the emergence of a gene regulatory function. Both the SET and the DNA transposase domains are involved in the different cellular roles of SETMAR, indicating the presence of novel and specific functions in anthropoid primates. In addition, SETMAR is dysregulated in different types of cancer, indicating a potential pathological role. While some light has been shed on SETMAR functions, more research and new tools are needed to better understand the cellular activities of SETMAR and to investigate the therapeutic potential of SETMAR.


SETMAR; Metnase; H3K36me2; Hsmar1; non-homologous end joining repair; NHEJ; transposase; transposable elements; histone; methyltransferase


Biology and Life Sciences, Biochemistry and Molecular Biology

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