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A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility
Noelia Fernández-Rivero1,2, Aitor Franco1,2, Adrian Velázquez-Campoy3,4,5,6
1Department of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country (UPV/EHU), P.O. Box 644, E-48080 Bilbao, Spain.
Scientific Reports
|August 26, 2016
Summary
Nucleoplasmin (NP) is a histone chaperone crucial for epigenome establishment. This study quantizes NP
Area of Science:
- Molecular Biology
- Epigenetics
- Chromatin Biology
Background:
- Nucleoplasmin (NP) is a major histone chaperone in vertebrate oocytes and embryos.
- NP plays a key role in establishing and maintaining the zygotic epigenome by managing maternal histones.
- Previous studies identified NP as an H2A-H2B chaperone, with recent evidence suggesting H3-H4 interaction, but quantitative data were lacking.
Purpose of the Study:
- To quantitatively investigate the interaction of Nucleoplasmin (NP) with different histone types (H2A-H2B, H3-H4, and linker histones).
- To explore the role of NP post-translational modifications in regulating histone binding affinity.
- To elucidate the mechanism of NP in chromatin remodeling, disassembly, and assembly.
Main Methods:
- Quantitative binding assays to determine dissociation constants (Kd) for NP-histone interactions.
- Analysis of NP post-translational modifications and their effect on the polyGlu tract and histone binding.
- Investigation of NP's interaction with H3-H4 in different conformations (dimers and tetramers) and its role in DNA binding.
Main Results:
- NP binds H2A-H2B, H3-H4, and linker histones with high affinity (subnanomolar Kd values), forming distinct complexes.
- Post-translational modifications of NP modulate the exposure of its polyGlu tract, enhancing affinity for all histones.
- NP binds H3-H4 tetramers and dimers, facilitating their transfer to DNA to form disomes and tetrasomes.
Conclusions:
- Nucleoplasmin exhibits broad histone chaperone activity, binding multiple histone types with high affinity.
- NP's interaction dynamics with H2A-H2B and linker histones, mediated by its distal face, are critical for sperm chromatin remodeling.
- NP's ability to bind and transfer H3-H4 complexes is significant for understanding its role in chromatin dynamics during replication and transcription.
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