A Novel Modification of the Lysine Residue at Position 12 of Histone H4 in Starfish Sperm.

Nunomura, K; Shimizu, T; Hozumi, K; Takao, T; Shimonishi, Y; Ikegami, S

Nunomura, K; Shimizu, T; Hozumi, K; Takao, T; Shimonishi, Y; Ikegami, S.

Afiliação

Nunomura K; a Department of Applied Biochemistry , Hiroshima University , 1-4-4 Kagamiyama, Higashi-hiroshima, Hiroshima 739 , Japan.
Shimizu T; a Department of Applied Biochemistry , Hiroshima University , 1-4-4 Kagamiyama, Higashi-hiroshima, Hiroshima 739 , Japan.
Hozumi K; a Department of Applied Biochemistry , Hiroshima University , 1-4-4 Kagamiyama, Higashi-hiroshima, Hiroshima 739 , Japan.
Takao T; a Department of Applied Biochemistry , Hiroshima University , 1-4-4 Kagamiyama, Higashi-hiroshima, Hiroshima 739 , Japan.
Shimonishi Y; b Institute for Protein Research, Osaka University , Suita, Osaka 565 , Japan.
Ikegami S; a Department of Applied Biochemistry , Hiroshima University , 1-4-4 Kagamiyama, Higashi-hiroshima, Hiroshima 739 , Japan.

Biosci Biotechnol Biochem ; 61(12): 2151-2, 1997 Jan.

Article em En | MEDLINE | ID: mdl-27396896

ABSTRACT

ABSTRACT

Post-translational modification of core histones is essential in processes requiring chromatin remodeling. We report here a novel modification in histones of the sperm of the starfish, Asterina pectinifera, which involves an Îµ-(Î³-glutamyl)lysine cross-link between the glutamine residue at position 9 of histone H2B and the lysine residue at position 12 of histone H4.

Palavras-chave

histone; starfish; transglutaminase

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: Biosci Biotechnol Biochem Assunto da revista: BIOQUIMICA / BIOTECNOLOGIA Ano de publicação: 1997 Tipo de documento: Article País de afiliação: Japão

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