Summary information and primary citation
- PDB-id
-
6vtx;
DSSR-derived features in text and
JSON formats
- Class
- DNA binding protein-DNA
- Method
- X-ray (2.14 Å)
- Summary
- Crystal structure of human klf4 zinc finger DNA binding
domain in complex with nanog DNA
- Reference
-
Sharma R, Choi KJ, Quan MD, Sharma S, Sankaran B, Park H,
LaGrone A, Kim JJ, MacKenzie KR, Ferreon ACM, Kim C,
Ferreon JC (2021): "Liquid
condensation of reprogramming factor KLF4 with DNA
provides a mechanism for chromatin organization."
Nat Commun, 12, 5579. doi:
10.1038/s41467-021-25761-7.
- Abstract
- Expression of a few master transcription factors can
reprogram the epigenetic landscape and three-dimensional
chromatin topology of differentiated cells and achieve
pluripotency. During reprogramming, thousands of long-range
chromatin contacts are altered, and changes in promoter
association with enhancers dramatically influence
transcription. Molecular participants at these sites have
been identified, but how this re-organization might be
orchestrated is not known. Biomolecular condensation is
implicated in subcellular organization, including the
recruitment of RNA polymerase in transcriptional
activation. Here, we show that reprogramming factor KLF4
undergoes biomolecular condensation even in the absence of
its intrinsically disordered region. Liquid-liquid
condensation of the isolated KLF4 DNA binding domain with a
DNA fragment from the NANOG proximal promoter is enhanced
by CpG methylation of a KLF4 cognate binding site. We
propose KLF4-mediated condensation as one mechanism for
selectively organizing and re-organizing the genome based
on the local sequence and epigenetic state.
