Fig. 2
An Arg-Trp amino acid substitution reduces the specific activity of Nipponbare OsNR2. a Amino acid substitution and insertion differences between the 9311 and Nipponbare OsNR2 proteins. Locations of conserved functional domains are indicated by green bars. b Constructs expressing chimeric OsNR2 proteins of varying amino acid sequence. Fragments from the 9311 and Nipponbare OsNR2 coding regions were exchanged to generate constructs encoding a series of four different chimeric OsNR2 proteins, differing with respect to the amino acid residues variant between 9311 and Nipponbare OsNR2. These constructs were expressed in E.coli. c Detection with anti:GST antibody (Cat No: CW0084M, CWBIOtech, Beijing, China) of OsNR2-GST fusion proteins extracted from E. coli and purified on a GST-sefinoseTM column (constructs as shown in b), showing roughly equivalent abundance of OsNR2 proteins. d NR activity of purified extracts as in b, c. Value is mean ± s.d. (n = 3). Error bar represents s.d. ** indicates the least significant difference at 0.01 probability level compared with Nipponbare. The source data underlying c and d are provided as a Source Data file
