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Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes

Yunsun Nam1, Piotr Sliz, Luyan Song

  • 1Biological and Biomedical Sciences Graduate Program in the Division of Medical Sciences, Harvard Medical School, Boston, MA 02115, USA.

Cell
|March 15, 2006
PubMed

Insights

This study reveals the crystal structure of a Notch transcriptional activation complex. This structure clarifies how Notch signaling precisely controls gene transcription during development.

Area of Science:

  • Cellular biology
  • Molecular biology
  • Structural biology

Background:

  • Notch receptors are crucial for cell-to-cell communication during development.
  • Signal transduction involves forming a complex that activates target gene transcription.

Purpose of the Study:

  • To determine the crystal structure of a Notch transcriptional activation complex.
  • To elucidate the molecular interactions governing Notch-mediated gene regulation.

Main Methods:

  • X-ray crystallography was used to obtain the structure.
  • The complex included the ankyrin domain of human Notch1 (ANK), CSL transcription factor, DNA, and Mastermind-like-1 (MAML-1).

Main Results:

  • The crystal structure reveals how ANK and CSL form a groove that binds MAML-1 as a helical structure.
  • This composite binding surface is critical for the precise recruitment of coactivators.

Conclusions:

  • The findings provide a structural basis for the regulated assembly of Notch:CSL complexes.
  • This mechanism ensures precise transcriptional control of Notch target genes, vital for developmental processes.

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