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Structural basis for LIN54 recognition of CHR elements in cell cycle-regulated promoters

Aimee H Marceau1, Jessica G Felthousen2, Paul D Goetsch3

  • 1Department of Chemistry and Biochemistry, University of California, 1156 High Street, Santa Cruz, California 95064, USA.

Nature Communications
|July 29, 2016
PubMed

Insights

The MuvB complex

Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Structural Biology

Background:

  • The MuvB complex regulates cell cycle-dependent gene expression.
  • LIN54 is a DNA-binding protein within the MuvB complex, targeting cell cycle genes homology region (CHR) elements.

Purpose of the Study:

  • To characterize the DNA-binding properties of LIN54.
  • To elucidate the structural basis for CHR sequence recognition by LIN54.

Main Methods:

  • Biochemical characterization of DNA-binding.
  • X-ray crystallography to determine the structure of LIN54 bound to DNA.
  • Demonstration of LIN54's role in MuvB recruitment.

Main Results:

  • The CHR consensus sequence was biochemically defined as TTYRAA.
  • Two tandem cysteine-rich regions in LIN54 are essential for high-affinity DNA binding.
  • Crystal structure revealed tyrosine residues mediating sequence-specific DNA binding in the minor groove.
  • Tyrosine-mediated DNA binding is crucial for MuvB recruitment to promoters.

Conclusions:

  • LIN54 utilizes a unique tyrosine-based mechanism for CHR DNA recognition.
  • MuvB may function by binding near transcription start sites and influencing nucleosome positioning.

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