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

Aimee H. Marceau, Jessica G. Felthousen, Paul D. Goetsch, Audra N. Iness, Hsiau-Wei Lee, Sarvind M. Tripathi, Susan Strome, Larisa Litovchick and Seth M. Rubin ()
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Aimee H. Marceau: University of California
Jessica G. Felthousen: Oncology and Palliative Care and Massey Cancer Center, Virginia Commonwealth University
Paul D. Goetsch: Cell and Developmental Biology, University of California
Audra N. Iness: Oncology and Palliative Care and Massey Cancer Center, Virginia Commonwealth University
Hsiau-Wei Lee: University of California
Sarvind M. Tripathi: University of California
Susan Strome: Cell and Developmental Biology, University of California
Larisa Litovchick: Oncology and Palliative Care and Massey Cancer Center, Virginia Commonwealth University
Seth M. Rubin: University of California

Nature Communications, 2016, vol. 7, issue 1, 1-11

Abstract: Abstract The MuvB complex recruits transcription factors to activate or repress genes with cell cycle-dependent expression patterns. MuvB contains the DNA-binding protein LIN54, which directs the complex to promoter cell cycle genes homology region (CHR) elements. Here we characterize the DNA-binding properties of LIN54 and describe the structural basis for recognition of a CHR sequence. We biochemically define the CHR consensus as TTYRAA and determine that two tandem cysteine rich regions are required for high-affinity DNA association. A crystal structure of the LIN54 DNA-binding domain in complex with a CHR sequence reveals that sequence specificity is conferred by two tyrosine residues, which insert into the minor groove of the DNA duplex. We demonstrate that this unique tyrosine-mediated DNA binding is necessary for MuvB recruitment to target promoters. Our results suggest a model in which MuvB binds near transcription start sites and plays a role in positioning downstream nucleosomes.

Date: 2016
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12301

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DOI: 10.1038/ncomms12301

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