Nucleosome assembly protein-1 is a linker histone chaperone in Xenopus eggs
| Autor: | Mari Iwabuchi, Hideaki Saeki, Keita Ohsumi, Keishi Shintomi, Kiyoe Ura, Takeo Kishimoto |
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| Jazyk: | angličtina |
| Rok vydání: | 2005 |
| Předmět: |
Cell Extracts
Male Xenopus Molecular Sequence Data Cell Cycle Proteins Biology Histones Histone H1 Histone methylation Histone H2A Animals Drosophila Proteins Histone code Amino Acid Sequence Histone octamer Histone binding Nucleosome Assembly Protein 1 Multidisciplinary Nuclear Proteins Proteins Biological Sciences Chromatin Assembly and Disassembly Spermatozoa Linker DNA Molecular biology Nucleosomes Cell biology Chromatosome Oocytes Female Molecular Chaperones |
| Zdroj: | Proc. Natl. Acad. Sci. USA. 102(No. 23):8210-8215 |
| Popis: | In eukaryotic cells, genomic DNA is primarily packaged into nucleosomes through sequential ordered binding of the core and linker histone proteins. The acidic proteins termed histone chaperones are known to bind to core histones to neutralize their positive charges, thereby facilitating their proper deposition onto DNA to assemble the core of nucleosomes. For linker histones, however, little has been known about the regulatory mechanism for deposition of linker histones onto the linker DNA. Here we report that, in Xenopus eggs, the linker histone is associated with the Xenopus homologue of nucleosome assembly protein-1 (NAP-1), which is known to be a chaperone for the core histones H2A and H2B in Drosophila and mammalian cells [Ito, T., Bulger, M., Kobayashi, R. & Kadonaga, J. T. (1996) Mol. Cell Biol. 16, 3112–3124; Chang, L., Loranger, S. S., Mizzen, C., Ernst, S. G., Allis, C. D. & Annunziato, A. T. (1997) Biochemistry 36, 469–480]. We show that NAP-1 acts as the chaperone for the linker histone in both sperm chromatin remodeling into nucleosomes and linker histone binding to nucleosome core dimers. In the presence of NAP-1, the linker histone is properly deposited onto linker DNA at physiological ionic strength, without formation of nonspecific aggregates. These results strongly suggest that NAP-1 functions as a chaperone for the linker histone in Xenopus eggs. |
| Databáze: | OpenAIRE |
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