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The polycomb protein MPc3 interacts with AF9, an MLL fusion partner in t(9;11)(p22;q23) acute leukemias

C S Hemenway1, A C de Erkenez, G C Gould

  • 1Department of Pediatrics, Tulane University School of Medicine, New Orleans, Louisiana, LA 70112, USA. chemenw@tulane.edu

Oncogene
|July 6, 2001
PubMed

Insights

Mouse Polycomb protein MPc3 binds the AF9 transcriptional activator, unlike related proteins. This suggests MPc3 may uniquely link gene silencing complexes to activators in cellular processes.

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Gene Regulation

Background:

  • Polycomb group (PcG) proteins form multiprotein complexes crucial for gene silencing.
  • PcG complexes exhibit heterogeneity in protein composition and function.
  • MPc3 is a mouse PcG protein homologous to M33 and MPc2, all binding RING1 via a C-box motif.

Purpose of the Study:

  • To investigate the interactions of the mouse Polycomb (Pc) protein MPc3 with other cellular proteins.
  • To determine if MPc3 interacts with AF9, a transcriptional activator involved in acute leukemias.
  • To elucidate the potential unique role of MPc3 within PcG complexes.

Main Methods:

  • Protein interaction studies were performed.
  • Mapping of binding sites within MPc3 and AF9 was conducted.

Main Results:

  • MPc3 directly interacts with the transcriptional activator AF9.
  • The carboxy-terminus of AF9 is the binding site for MPc3.
  • MPc3's AF9 binding site is in a central, non-conserved region.
  • The related Pc protein M33 does not interact with AF9.

Conclusions:

  • MPc3 possesses a unique interaction capability with the transcriptional activator AF9.
  • This interaction suggests a novel mechanism for linking PcG gene silencing machinery to transcriptional activation pathways.
  • MPc3 may play a distinct role in regulating gene expression, particularly in contexts like acute leukemia.

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