Structure, activity, and function of SETMAR protein lysine methyltransferase

Journal article : Review

Abstract:: 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.

Files:: Tellier_2022_Structure_Activity_Function.pdf

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Language:: English
Keywords:: Hsmar1

histone

H3K36me2

non-homologous end joining repair

NHEJ

Metnase

transposase

transposable elements

methyltransferase

FFR

SETMAR
Subtype:: Review
Pubs id:: 1231420
Local pid:: pubs:1231420
Deposit date:: 2022-08-03
ARK identifier:: ark:/29072/ora_457f9377da1a41d9a1496addbd7b4cfe

Copyright holder:: Michael Tellier
Rights statement:: ©2021 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https:// creativecommons.org/licenses/by/ 4.0/).

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