The BRI1 protein contains a hydrophobic signal peptide at the N-t

The BRI1 protein contains a hydrophobic signal peptide at the N-terminus, an extracellular leucine-rich repeat (LRRs) domain interrupted by a non-repetitive island domain, a transmembrane domain, and a cytoplasmic serine/threonine kinase domain [18] and [19]. The kinase activity of BRI1 is essential for BR regulation of plant growth and development in rice [20]. The N-terminal signal peptide is likely to be required for translocation of the nascent

protein across a membrane, while the transmembrane JQ1 mw domain is required to anchor the protein in the plasma membrane [21]. The island domain and the adjacent C-terminal LRR repeat of the extracellular domain are responsible for perceiving BRs [22], [23] and [24]. The LRR domain may be involved in facilitating

protein–protein interactions between individual BRI1 molecules or with other proteins such as BAK1 [25]. BR binding can enhance BRI1 heteromerization with BAK1 (BRI1-associated kinase 1), another LRR-RLK that is localized to the plasma membrane [25]. In Arabidopsis, BAK1 and BRI1 share similar gene expression and subcellular localization patterns and physically associate with each other. BAK1/BRI1 interaction activates their kinase activities through transphosphorylation [26]. Structure analysis reveals that BAK1 acts as a co-receptor to recognize the BRI1-bound brassinolide and the extracellular domains of BRI1 and BAK1 interact with each other in a BL- and pH-dependent manner [27]. According to the solved crystal structure of the BRI1LRR-BL-BAK1LRR complex, the C-terminal two LRRs of BRI1LRR make extensive and direct Selleckchem Epigenetic inhibitor contact with BAK1LRR [27].

Thus the structural stability of Forskolin nmr the BRI1 LRR domain is very important for both BR perception and association with the co-receptor BAK1. In the present study we characterized a classic semi-dwarf mutant with erect leaves in rice, designated as gsor300084. gsor300084 was insensitive to BRs and shown to be an allelic mutant of D61 (OsBRI1). A point mutation in the LRR domain was found in the gsor300084 mutant. The potential effect of this mutation on BRI1 protein structure and function is discussed. The gsor300084 mutant and the wild-type variety Matsumae (Oryza sativa ssp. japonica, cv. Matsumae) were kindly provided by the USDA-ARS Dale Bumpers National Rice Research Center. The rice plants were grown in a paddy field at the experimental station of the Shandong Rice Research Institute, Shandong, China. Rice seeds were soaked in water for 24 h and then sprouted at 37 °C. Well-germinated seeds were transferred into 96-well plates supplemented with water and grown in the dark at 28 °C for 20 days. Seeds of the gsor300084 mutant and Matsumae were grown in half-strength MS solid medium with 0 or 1 μmol L− 1 BL in a dark growth chamber at 28 °C for 4 days. Coleoptile and root elongation analysis was performed by measuring the length of coleoptile and root treated with or without BL.

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