Fig. 4

OsSAPK9 interactions with different OsSGT1 domains in vitro and in vivo. a Schematic of the functional domain of OsSGT1. Positions of the tetratricopeptide repeat (TPR) domain (1–167 amino acids), the CHORD-containing protein and SGT1 (CS) domain (108–284 amino acids), the SGT-specific (SGS) domain (245–367 amino acids), the ΔTPR domain (108–367 amino acids), and the ΔSGS domain (1–284 amino acids) are indicated. b OsSAPK9 interactions with the TPR and CS domains in yeast. The TPR, CS, SGS, ΔTPR, and ΔSGS domains are from OsSGT1. AH109 yeast transformants diluted 10, 100, 1000, or 10,000 times were plated on synthetic dextrose (SD) medium lacking Trp and Leu amino acids (SD − L/T) or SD medium lacking Trp, Leu, His and Ade amino acids (SD − L/T/W/A). c OsSAPK9 bound to the TPR domain of OsSGT1 in the glutathione S-transferase (GST) pull-down assay involving His-OsSAPK9 and GST-TPR. d OsSAPK9 bound to the CS domains of OsSGT1 in the glutathione S-transferase (GST) pull-down assay involving His-OsSAPK9 and GST-CS. e OsSAPK9 interactions with the TPR and CS domains in a bimolecular fluorescence complementation assay. OsSAPK9 was fused to an N-terminal yellow fluorescent protein (NYFP-OsSAPK9), and TPR, CS, SGS, ΔTPR, and ΔSGS were fused to C-terminal cyan fluorescent proteins (CCFP-TPR, CCFP-CS, CCFP-SGS, CCFP-ΔTPR, and CCFP-ΔSGS). f OsSAPK9 interactions with OsHsp90 in the bimolecular fluorescence complementation assay. OsSAPK9 was fused to an N-terminal yellow fluorescent protein (NYFP-OsSAPK9), and OsHsp90 was fused to a C-terminal cyan fluorescent protein (CCFP-Hsp90). g OsSAPK9 bound to OsHsp90 in the GST pull-down assay involving His-OsSAPK9 and GST-OsHsp90