Structural basis of recognition and destabilization of the histone H2B ubiquitinated nucleosome by the DOT1L histone H3 Lys79 methyltransferase.

Jang, Seongmin; Kang, Chanshin; Yang, Han-Sol; Jung, Taeyang; Hebert, Hans; Chung, Ka Young; Kim, Seung Joong; Hohng, Sungchul; Song, Ji-Joon

Jang, Seongmin; Kang, Chanshin; Yang, Han-Sol; Jung, Taeyang; Hebert, Hans; Chung, Ka Young; Kim, Seung Joong; Hohng, Sungchul; Song, Ji-Joon.

Afiliação

Jang S; Department of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Korea.
Kang C; Department of Physics and Astronomy, Seoul National University, Seoul 08826, Korea.
Yang HS; School of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Jung T; School of Engineering Sciences in Chemistry, Biotechnology, and Health, Department of Biomedical Engineering and Health Systems, KTH Royal Institute of Technology, S-141 52 Huddinge, Sweden.
Hebert H; Department of Biosciences and Nutrition, Karolinska Institutet, S-141 52 Huddinge, Sweden.
Chung KY; School of Engineering Sciences in Chemistry, Biotechnology, and Health, Department of Biomedical Engineering and Health Systems, KTH Royal Institute of Technology, S-141 52 Huddinge, Sweden.
Kim SJ; Department of Biosciences and Nutrition, Karolinska Institutet, S-141 52 Huddinge, Sweden.
Hohng S; School of Pharmacy, Sungkyunkwan University, Suwon 16419, Korea.
Song JJ; Department of Physics, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Korea.

Genes Dev ; 33(11-12): 620-625, 2019 06 01.

Article em En | MEDLINE | ID: mdl-30923167

Assuntos

Histonas/química; Histonas/metabolismo; Metiltransferases/química; Metiltransferases/metabolismo; Nucleossomos/química; Nucleossomos/metabolismo; Arginina/metabolismo; Domínio Catalítico; Microscopia Crioeletrônica; Histona-Lisina N-Metiltransferase/química; Histona-Lisina N-Metiltransferase/metabolismo; Humanos; Interações Hidrofóbicas e Hidrofílicas; Metilação; Modelos Moleculares; Estabilidade Proteica; Estrutura Secundária de Proteína; Ubiquitina/metabolismo; Ubiquitinação

Palavras-chave

cryo-EM; histone; methylation; nucleosome; ubiquitin

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Histonas / Nucleossomos / Metiltransferases Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Revista: Genes Dev Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2019 Tipo de documento: Article

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