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Structural insight into the zinc finger CW domain as a histone modification reader
Fahu He1, Takashi Umehara, Kohei Saito
1RIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan.
Structure (London, England : 1993)
|September 10, 2010
Summary
The zinc finger CW (zf-CW) domain, found in epigenetic regulators, has a novel structure. This study reveals its histone H3 binding mode, identifying it as a key epigenetic reader module.
Area of Science:
- Structural biology
- Epigenetics
- Molecular biology
Background:
- The zinc finger CW (zf-CW) domain is a conserved motif implicated in epigenetic regulation.
- ZCWPW1 is a human protein containing both zf-CW and PWWP domains.
Purpose of the Study:
- To determine the NMR solution structure of the zf-CW domain of ZCWPW1.
- To elucidate the binding mechanism of the zf-CW domain to histone modifications.
Main Methods:
- Nuclear Magnetic Resonance (NMR) spectroscopy to determine the solution structure.
- Biochemical assays to study protein-peptide interactions.
Main Results:
- The zf-CW domain exhibits a new fold with tetrahedral zinc coordination by four cysteine residues.
- Its structure resembles the plant homeo domain (PHD) finger, suggesting functional similarity.
- The structure of the zf-CW domain complexed with histone H3 tail peptide (1-10) trimethylated at K4 was determined, clarifying the binding mode.
Conclusions:
- The zf-CW domain possesses a unique fold and functions as a histone modification reader.
- This finding expands the repertoire of epigenetic reader modules involved in gene regulation.
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