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SnRK1 regulates chromatin-associated OXS3 family proteins localization through phosphorylation in Arabidopsis thaliana.
Xiao, Shimin; Jiang, Li; Wang, Changhu; Ow, David W.
Afiliação
  • Xiao S; Plant Gene Engineering Center, Chinese Academy of Sciences Key Laboratory of South China Agricultural Plant Molecular Analysis and Genetic Improvement, Guangdong Key Laboratory of Applied Botany, South China Botanical Garden, Chinese Academy of Sciences, Guangzhou, China; University of Chinese Acade
  • Jiang L; Plant Gene Engineering Center, Chinese Academy of Sciences Key Laboratory of South China Agricultural Plant Molecular Analysis and Genetic Improvement, Guangdong Key Laboratory of Applied Botany, South China Botanical Garden, Chinese Academy of Sciences, Guangzhou, China; University of Chinese Acade
  • Wang C; Plant Gene Engineering Center, Chinese Academy of Sciences Key Laboratory of South China Agricultural Plant Molecular Analysis and Genetic Improvement, Guangdong Key Laboratory of Applied Botany, South China Botanical Garden, Chinese Academy of Sciences, Guangzhou, China. Electronic address: cwang@s
  • Ow DW; Plant Gene Engineering Center, Chinese Academy of Sciences Key Laboratory of South China Agricultural Plant Molecular Analysis and Genetic Improvement, Guangdong Key Laboratory of Applied Botany, South China Botanical Garden, Chinese Academy of Sciences, Guangzhou, China. Electronic address: dow@scb
Biochem Biophys Res Commun ; 533(3): 526-532, 2020 12 10.
Article em En | MEDLINE | ID: mdl-32981682
ABSTRACT
In plants, SNF1-related protein kinase 1 (SnRK1) senses nutrient and energy status and transduces this information into appropriate responses. Oxidative Stress 3 (OXS3) and family members share a highly conserved putative N-acetyltransferase catalytic domain (ACD). Here, we describe that the ACD contains two candidate SnRK1 recognition motifs and that SnRK1 can interact with most of the OXS3 family proteins. In vitro, SnRK1.1 can phosphorylate OXS3, OXS3b and O3L4, and in vivo promote the translocation of OXS3, OXS3b and O3L6 from the nucleus to the cytoplasm. Phosphorylation sites within the OXS3 ACD affect OXS3 cytoplasmic accumulation, as well as their interactions with SnRK1.1. This suggests that signal transduction from SnRK1 to OXS3 family proteins, and that SnRK1 can control their activities through phosphorylation-induced nuclear exclusion.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas Serina-Treonina Quinases / Proteínas de Arabidopsis Tipo de estudo: Risk_factors_studies Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas Serina-Treonina Quinases / Proteínas de Arabidopsis Tipo de estudo: Risk_factors_studies Idioma: En Ano de publicação: 2020 Tipo de documento: Article