How Histone Chaperones Nap1 and Vps75 Bind Histones H3 and H4
Author Information
Author(s): Andrew Bowman, Richard Ward, Nicolas Wiechens, Vijender Singh, Hassane El-Mkami, David George Norman, Tom Owen-Hughes
Primary Institution: Wellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, UK
Hypothesis
Nap1 and Vps75 can bind histones H3 and H4 in their tetrameric conformation.
Conclusion
Nap1 and Vps75 are capable of binding histones H3 and H4 as a tetramer, which may help maintain histone integrity during DNA replication.
Supporting Evidence
- Nap1 and Vps75 can bind all four core histones with high affinity.
- Histones H3 and H4 remain in a tetrameric conformation when bound to Nap1 and Vps75.
- Nap1 can deposit a whole (H3-H4)2 tetramer onto DNA.
- Vps75-Rtt109 preferentially acetylates tetrameric H3 and H4.
Takeaway
This study shows that two proteins, Nap1 and Vps75, can hold histones together in a special way that helps them work better when making DNA.
Methodology
The study used pulsed electron double resonance (PELDOR) measurements and protein crosslinking to analyze the binding of histones H3 and H4 to Nap1 and Vps75.
Limitations
The study does not rule out the possibility that under certain conditions, histones may bind as dimers instead of tetramers.
Digital Object Identifier (DOI)
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