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Key residues for maintaining architecture, assembly of plant hormone SA receptor NPR1.
Ji, Chaoguang; Yang, Wenbo; Wang, Yongan; Su, Chunlin; Li, Xiaorui; Liu, Peiyuan; Yan, Hanchi.
Afiliación
  • Ji C; School of Life Sciences, Tianjin University, Tianjin, 300072, China.
  • Yang W; School of Life Sciences, Tianjin University, Tianjin, 300072, China.
  • Wang Y; School of Life Sciences, Tianjin University, Tianjin, 300072, China.
  • Su C; School of Life Sciences, Tianjin University, Tianjin, 300072, China.
  • Li X; School of Life Sciences, Tianjin University, Tianjin, 300072, China.
  • Liu P; School of Life Sciences, Tianjin University, Tianjin, 300072, China. Electronic address: peiyuan.liu@tju.edu.cn.
  • Yan H; School of Life Sciences, Tianjin University, Tianjin, 300072, China. Electronic address: hanchi.yan@tju.edu.cn.
Biochem Biophys Res Commun ; 613: 94-99, 2022 07 12.
Article en En | MEDLINE | ID: mdl-35550200
ABSTRACT
Salicylic acid (SA) is a pivotal hormone required for the development of resistance to many pathogens in plants. As an SA receptor, NPR1(Nonexpressor of Pathogenesis-Related Genes 1) plays a key regulatory role in the plant immune response. The function of NPR1 is dependent on the alteration of its oligomer-to-monomer. Research in recent years has proven that NPRs perceive SA and regulate the expression of downstream defense genes, but the mechanism of NPR1 oligomer-to-monomer conversion remains unclear. In this paper, we mainly studied the oligomerization of NPR1. By mutation experiments on some residues in the BTB domain involved in protein interactions, we found that the residue His80 plays a key role in the oligomerization of NPR1. We also found that NPR1, interacting with zinc ions at a ratio close to 11, was independent of the residue His80. These findings may help us to understand the conformational conversion of NPR1.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Arabidopsis / Proteínas de Arabidopsis Idioma: En Revista: Biochem Biophys Res Commun Año: 2022 Tipo del documento: Article País de afiliación: China

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Arabidopsis / Proteínas de Arabidopsis Idioma: En Revista: Biochem Biophys Res Commun Año: 2022 Tipo del documento: Article País de afiliación: China