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Titolo:
Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation
Autore:
Goto, H; Tomono, Y; Ajiro, K; Kosako, H; Fujita, M; Sakurai, M; Okawa, K; Iwamatsu, A; Okigaki, T; Takahashi, T; Inagaki, M;
Indirizzi:
Aichi Canc Ctr, Res Inst, Biochem Lab, Chikusa Ku, Nagoya, Aichi 4648681, Japan Aichi Canc Ctr Nagoya Aichi Japan 4648681 u, Nagoya, Aichi 4648681, Japan Aichi Canc Ctr, Res Inst, Cell Biol Lab, Chikusa Ku, Nagoya, Aichi 4648681, Japan Aichi Canc Ctr Nagoya Aichi Japan 4648681 u, Nagoya, Aichi 4648681, Japan Aichi Canc Ctr, Res Inst, Lab Viral Oncol, Chikusa Ku, Nagoya, Aichi 4648681, Japan Aichi Canc Ctr Nagoya Aichi Japan 4648681 u, Nagoya, Aichi 4648681, Japan Aichi Canc Ctr, Res Inst, Immunol Lab, Chikusa Ku, Nagoya, Aichi 4648681, Japan Aichi Canc Ctr Nagoya Aichi Japan 4648681 u, Nagoya, Aichi 4648681, Japan Shigei Med Res Inst, Div Cell & Mol Biol, Okayama 7010202, Japan Shigei Med Res Inst Okayama Japan 7010202 l Biol, Okayama 7010202, Japan Mie Univ, Sch Med, Dept Pediat, Tsu, Mie 5148507, Japan Mie Univ Tsu Mie Japan 5148507 Med, Dept Pediat, Tsu, Mie 5148507, Japan Kirin Brewery Co Ltd, Cent Labs Key Technol, Yokohama, Kanagawa 2360004, Japan Kirin Brewery Co Ltd Yokohama Kanagawa Japan 2360004 agawa 2360004, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 36, volume: 274, anno: 1999,
pagine: 25543 - 25549
SICI:
0021-9258(19990903)274:36<25543:IOANPS>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
RHO-ASSOCIATED KINASE; FIBRILLARY ACIDIC PROTEIN; CELL-CYCLE; CHROMATIN CONDENSATION; LINKER HISTONES; INTERMEDIATE FILAMENTS; MITOSIS; DNA; H1; INVITRO;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
56
Recensione:
Indirizzi per estratti:
Indirizzo: Inagaki, M Aichi Canc Ctr, Res Inst, Biochem Lab, Chikusa Ku, 1-1 Kanokoden, Nagoya, Aichi 4648681, Japan Aichi Canc Ctr 1-1 Kanokoden Nagoya Aichi Japan 4648681 , Japan
Citazione:
H. Goto et al., "Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation", J BIOL CHEM, 274(36), 1999, pp. 25543-25549

Abstract

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 P-32-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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 10:13:35