<i>S</i>-Glutathionylation of human inducible Hsp70 reveals a regulatory mechanism involving the C-terminal &#945;-helical lid.

Yang, Jie; Zhang, Hong; Gong, Weibin; Liu, Zhenyan; Wu, Huiwen; Hu, Wanhui; Chen, Xinxin; Wang, Lei; Wu, Si; Chen, Chang; Perrett, Sarah

S-Glutathionylation of human inducible Hsp70 reveals a regulatory mechanism involving the C-terminal α-helical lid.

Yang, Jie; Zhang, Hong; Gong, Weibin; Liu, Zhenyan; Wu, Huiwen; Hu, Wanhui; Chen, Xinxin; Wang, Lei; Wu, Si; Chen, Chang; Perrett, Sarah.

Afiliação

Yang J; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Chaoyang District, Beijing, China.
Zhang H; University of the Chinese Academy of Sciences, Shijingshan District, Beijing, China.
Gong W; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Chaoyang District, Beijing, China zhangh@moon.ibp.ac.cn changchen@moon.ibp.ac.cn sarah.perrett@cantab.net.
Liu Z; University of the Chinese Academy of Sciences, Shijingshan District, Beijing, China.
Wu H; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Chaoyang District, Beijing, China.
Hu W; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Chaoyang District, Beijing, China.
Chen X; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Chaoyang District, Beijing, China.
Wang L; University of the Chinese Academy of Sciences, Shijingshan District, Beijing, China.
Wu S; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Chaoyang District, Beijing, China.
Chen C; University of the Chinese Academy of Sciences, Shijingshan District, Beijing, China.
Perrett S; National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Chaoyang District, Beijing, China.

J Biol Chem ; 295(24): 8302-8324, 2020 06 12.

Article em En | MEDLINE | ID: mdl-32332101

Assuntos

Glutationa/metabolismo; Proteínas de Choque Térmico HSP70/química; Proteínas de Choque Térmico HSP70/metabolismo; Sítios de Ligação; Biotina/metabolismo; Cisteína/metabolismo; Proteínas de Choque Térmico HSP70/genética; Células HeLa; Humanos; Espectroscopia de Ressonância Magnética; Proteínas Mutantes/química; Proteínas Mutantes/metabolismo; Mutação/genética; Peptídeos/química; Peptídeos/metabolismo; Estabilidade Proteica; Estrutura Secundária de Proteína; Desdobramento de Proteína; Relação Estrutura-Atividade; Especificidade por Substrato

Palavras-chave

70-kilodalton heat shock protein (Hsp70); HspA1A; chaperone; cysteine modification; disulfide bond; glutathionylation; oxidative stress; protein homeostasis; protein structure

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Choque Térmico HSP70 / Glutationa Limite: Humans Idioma: En Revista: J Biol Chem Ano de publicação: 2020 Tipo de documento: Article País de afiliação: China

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