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Identification of a Novel Phosphorylation Site on Histone H3 Coupled with Mitotic Chromosome Condensation
Open accessAbstract
Histone H3 (H3) phosphorylation at Ser(10) occurs during mitosis in eukaryotes and was recently shown to play an important role in chromosome condensation in Tetrahymena. When producing monoclonal antibodies that recognize glial fibrillary acidic protein phosphorylation at Thr(7), we obtained some monoclonal antibodies that cross-reacted with early mitotic chromosomes. They reacted with 15-kDa phosphoprotein specifically in mitotic cell lysate. With microsequencing, this phosphoprotein was proved to be H3. Mutational analysis revealed that they recognized H3 Ser(28) phosphorylation. Then we produced a monoclonal antibody, HTA28, using a phosphopeptide corresponding to phosphorylated H3 Ser(28). This antibody specifically recognized the phosphorylation of H3 Ser(28) but not that of glial fibrillary acidic protein Thr(7). Immunocytochemical studies with HTA28 revealed that Ser(28) phosphorylation occurred in chromosomes predominantly during early mitosis and coincided with the initiation of mitotic chromosome condensation. Biochemical analyses using (32)P-labeled mitotic cells also confirmed that H3 is phosphorylated at Ser(28) during early mitosis. In addition, we found that H3 is phosphorylated at Ser(28) as well as Ser(10) when premature chromosome condensation was induced in tsBN2 cells. These observations suggest that H3 phosphorylation at Ser(28), together with Ser(10), is a conserved event and is likely to be involved in mitotic chromosome condensation.
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Cites
An acidic protein isolated from fibrous astrocytes
Eng, L. F., Vanderhaeghen, J. J., Bignami, A., & Gerstl, B. (1971) · Brain Research · doi:10.1016/0006-8993(71)90668-8 · Cited by 1,230
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The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679
Signaling to Chromatin through Histone Modifications
Cheung, P., Allis, C. D., & Sassone-Corsi, P. (2000) · Cell · doi:10.1016/s0092-8674(00)00118-5 · Cited by 989
Kunath, T., Saba-El-Leil, M. K., Almousailleakh, M., Wray, J., Meloche, S., & Smith, A. (2007) · Development · doi:10.1242/dev.02880 · Cited by 801
Tachibana, M., Sugimoto, K., Fukushima, T., & Shinkai, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101914200 · Cited by 784
Mitotic Phosphorylation of Histone H3: Spatio-Temporal Regulation by Mammalian Aurora Kinases
Crosio, C., Fimia, G. M., Loury, R., Kimura, M., Okano, Y., Zhou, H., Sen, S., Allis, C. D., & Sassone-Corsi, P. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.3.874-885.2002 · Cited by 666
Metadata
- Authors
- Goto, H., Kosako, H., Tomono, Y., Ajiro, K., Fujita, M., Sakurai, M., Okawa, K., Iwamatsu, A., Okigaki, T., Takahashi, T., & Inagaki, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-09
- Volume
- 274
- Issue
- 36
- Pages
- 25543-25549
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2108408221
- Cited by
- 457
- References
- 1
- FWCI
- 4.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- The paper
- Goto, H., Kosako, H., Tomono, Y., Ajiro, K., Fujita, M., Sakurai, M., Okawa, K., Iwamatsu, A., Okigaki, T., Takahashi, T., & Inagaki, M. (1999). Identification of a Novel Phosphorylation Site on Histone H3 Coupled with Mitotic Chromosome Condensation. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.274.36.25543
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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