Structure and function of histone acetyltransferase MOF

Qiao Yi Chen1, Max Costa1, Hong Sun1

  • 1Department of Environmental Medicine, NYU School of Medicine, Tuxedo, NY, USA.

AIMS Biophysics
|May 16, 2017
PubMed

Insights

The male-specific lethal complex member MOF (male-specific lethal complex component MSL, also known as MYST1) is a histone acetyltransferase. This review discusses hMOF

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Biochemistry

Background:

  • The MOF protein, initially identified in Drosophila melanogaster, is a key component of the dosage compensation complex.
  • As a member of the MYST family of histone acetyltransferases, MOF specifically targets histone H4 lysine 16 for acetylation.
  • Mammalian orthologs of MOF have conserved substrate specificity and enzymatic activities, highlighting its evolutionary importance.

Purpose of the Study:

  • To review the structure and activity of mammalian hMOF.
  • To discuss the role of hMOF in H4K16 acetylation, DNA damage response, and stem cell pluripotency.
  • To explore the implications of hMOF dysregulation in human carcinogenesis.

Main Methods:

  • Literature review of existing studies on MOF and hMOF.
  • Analysis of conserved features and functions across species.
  • Synthesis of data on hMOF's involvement in various cellular processes and diseases.

Main Results:

  • hMOF is crucial for regulating gene expression, DNA repair, and maintaining stem cell pluripotency.
  • Specific acetylation of H4K16 by hMOF is a key mechanism in its diverse functions.
  • Dysregulation of hMOF is linked to the development and progression of various human cancers.

Conclusions:

  • hMOF plays a vital role in fundamental biological processes, including epigenetic regulation and DNA damage response.
  • Understanding hMOF's functions offers insights into potential therapeutic strategies for cancer.
  • Further research into hMOF's mechanisms can illuminate its broader roles in health and disease.

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