SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is methylated in vivo

Soumen Chakraborty1, Kislay Kumar Sinha, Vitalyi Senyuk

  • 1Department of Pathology and The Cancer Center, University of Illinois at Chicago, Chicago, IL 60607, USA.

Oncogene
|August 15, 2003
PubMed

Insights

The histone methyltransferase SUV39H1 interacts with Acute Myeloid Leukemia 1 (AML1), a key gene regulator. This interaction inhibits AML1

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Hematopoiesis

Background:

  • Acute Myeloid Leukemia 1 (AML1) is a crucial DNA-binding protein regulating hematopoietic gene expression.
  • AML1 is essential for fetal liver hematopoiesis in mice.
  • Previous studies show AML1 interacts with histone acetyltransferases and deacetylases.

Purpose of the Study:

  • To investigate the interaction between AML1 and histone methyltransferase SUV39H1.
  • To understand how SUV39H1 affects AML1's function in gene regulation.

Main Methods:

  • Co-immunoprecipitation assays to detect protein complexes.
  • Analysis of AML1 N-terminus and Runt domain involvement.
  • Assessment of AML1's DNA-binding and transactivating properties.

Main Results:

  • SUV39H1 forms a complex with AML1.
  • The interaction requires AML1's N-terminus, including the Runt domain.
  • SUV39H1 binding abrogates AML1's DNA-binding and transactivating capabilities.
  • AML1's nuclear structure is disrupted upon binding to SUV39H1.

Conclusions:

  • SUV39H1 negatively regulates AML1 activity.
  • Histone methyltransferases are involved in modulating AML1's gene regulatory functions.
  • This interaction provides new insights into epigenetic control of hematopoiesis.

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