Characterization of Human PWWP Domains
Author Information
Author(s): Wu Hong, Zeng Hong, Lam Robert, Tempel Wolfram, Amaya Maria F., Xu Chao, Dombrovski Ludmila, Qiu Wei, Wang Yanming, Min Jinrong
Primary Institution: Structural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada
Hypothesis
The PWWP domain has the potential to bind histones and exhibits dual functions in binding both DNA and methyllysine histones.
Conclusion
PWWP proteins constitute a new family of methyl lysine histone binders, exhibiting dual functions in binding both DNA and methyllysine histones.
Supporting Evidence
- The PWWP domain was shown to exhibit histone binding ability only recently.
- Fluorescence polarization studies indicated weak histone binding ability of PWWP domains.
- Crystal structures of PWWP domains in complex with methylated histones were determined.
Takeaway
The PWWP domain can stick to both DNA and special types of histones, which are proteins that help package DNA in cells.
Methodology
The study used protein family approaches to determine crystal structures and fluorescence polarization binding studies to assess histone binding ability.
Digital Object Identifier (DOI)
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