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Requirement for multiple domains of the protein arginine methyltransferase CARM1 in its transcriptional coactivator

Catherine Teyssier1, Dagang Chen, Michael R Stallcup

  • 1Department of Pathology, University of Southern California, Los Angeles, California 90089, USA.

The Journal of Biological Chemistry
|September 28, 2002
PubMed

Insights

The coactivator-associated arginine methyltransferase 1 (CARM1) complex is vital for gene activation. Beyond its methyltransferase role, CARM1

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Gene Regulation

Background:

  • The p160 coactivator complex is essential for transcriptional activation mediated by nuclear receptors and other DNA-binding proteins.
  • This complex comprises p160 coactivators (e.g., SRC-1, GRIP1), histone acetyltransferases (e.g., CBP, p300), and the histone methyltransferase CARM1.
  • CARM1, CBP, and p300 collaboratively remodel chromatin structure and recruit RNA polymerase II through protein methylation and acetylation.

Purpose of the Study:

  • To investigate the functional domains of CARM1 beyond its methyltransferase activity in transcriptional coactivation.
  • To elucidate the specific roles of CARM1's conserved central region and unique N- and C-terminal regions in gene activation.

Main Methods:

  • Analysis of CARM1 domains for methyltransferase, binding, and homo-oligomerization activities.
  • Assessment of CARM1's N- and C-terminal regions for their contribution to transcriptional activation by nuclear receptors.
  • Identification of potential protein-protein interactions mediated by CARM1's C-terminal activation domain.

Main Results:

  • CARM1 possesses distinct domains required for coactivator function, in addition to its methyltransferase activity.
  • The central region of CARM1 harbors methyltransferase, binding, and homo-oligomerization activities and is highly conserved.
  • Both N- and C-terminal regions of CARM1 are necessary for enhancing nuclear receptor-mediated transcription; the C-terminus contains an autonomous activation domain.

Conclusions:

  • CARM1's coactivator function is multifaceted, involving its methyltransferase activity and contributions from its unique terminal regions.
  • The central conserved domain and the C-terminal activation domain play critical roles in CARM1's interaction with the transcription machinery.
  • CARM1 likely interacts with other proteins via its C-terminal domain to effectively mediate transcriptional coactivation.

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