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sNASP and ASF1A function through both competitive and compatible modes of histone binding
Andrew Bowman1, Akiko Koide2,3, Jay S Goodman2
1Biomedical Center Munich, Physiological Chemistry, Faculty of Medicine, Ludwig-Maximilians-Universität München, Großhaderner Str. 9, 82152 Planegg-Martinsried, Germany a.bowman.1@warwick.ac.uk.
Nucleic Acids Research
|January 27, 2017
Summary
Histone chaperones sNASP and ASF1 form a quaternary complex with histones H3-H4, revealing a network of interactions essential for nucleosome assembly. This study elucidates how these proteins cooperate to facilitate histone entry into the nucleosome pathway.
Area of Science:
- Molecular Biology
- Epigenetics
- Protein Interactions
Background:
- Histone chaperones are crucial for nucleosome assembly, a fundamental process in DNA regulation.
- sNASP and ASF1 are conserved histone chaperones interacting with histones H3 and H4.
- Previous work identified a shared binding site for sNASP and ASF1 on histone H3.
Purpose of the Study:
- To investigate how sNASP and ASF1 coexist in a complex with histones H3 and H4.
- To elucidate the interaction network between sNASP, ASF1, and histones H3-H4.
- To understand the sequential roles of sNASP and ASF1 in histone chaperone pathways.
Main Methods:
- Biochemical assays to identify histone interaction sites on sNASP.
- In vitro complex formation studies with sNASP, ASF1, and histones H3-H4.
- Analysis of quaternary complex formation and histone dimer folding.
Main Results:
- sNASP possesses additional histone interaction surfaces compatible with ASF1A binding.
- ASF1A can form a quaternary complex with sNASP and H3-H4.
- sNASP forms a complex with H3 independently, suggesting an upstream role to ASF1A.
- sNASP and ASF1A cooperatively fold H3-H4 dimers in vitro.
Conclusions:
- A network of binding events involving sNASP and ASF1 facilitates histone H3-H4 entry into the nucleosome assembly pathway.
- sNASP may act upstream of ASF1A in the histone deposition process.
- The findings provide new insights into the mechanism of nucleosome formation.
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