Limits...
Three genes encoding AOP2, a protein involved in aliphatic glucosinolate biosynthesis, are differentially expressed in Brassica rapa.

Zhang J, Liu Z, Liang J, Wu J, Cheng F, Wang X - J. Exp. Bot. (2015)

Bottom Line: Site-directed mutagenesis showed that His356, Asp310, and Arg376 residues are required for the catalytic activity of one of the BrAOP2 proteins (BrAOP2.1).Promoter-β-glucuronidase lines revealed that the BrAOP2.3 gene displayed an overlapping but distinct tissue- and cell-specific expression profile compared with that of the BrAOP2.1 and BrAOP2.2 genes.Taken together, our results revealed that all three BrAOP2 paralogues are active in B. rapa but have functionally diverged.

View Article: PubMed Central - PubMed

Affiliation: Institute of Vegetables and Flowers, Chinese Academy of Agricultural Sciences, Zhongguancun Nandajie No. 12, Haidian District, Beijing 100081, PR China.

No MeSH data available.


Four active-site residues identified in three BrAOP2 2OG-FeII_Oxy domains. The tertiary structure of each BrAOP2 protein was predicted with the program SWISS-MODEL, and the representation was made with Swiss Pdb-Viewer 4.01 (Arnold et al, 2006). (This figure is available in colour at JXB online.)
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License 1 - License 2
getmorefigures.php?uid=PMC4588880&req=5

Figure 7: Four active-site residues identified in three BrAOP2 2OG-FeII_Oxy domains. The tertiary structure of each BrAOP2 protein was predicted with the program SWISS-MODEL, and the representation was made with Swiss Pdb-Viewer 4.01 (Arnold et al, 2006). (This figure is available in colour at JXB online.)

Mentions: The two conserved domains DIOX-N and 2OG-FeII_Oxy at the N- and C-terminal regions of BrAOP2 (Fig. 2) are essential for 2-oxoglutarate/Fe(II)-dependent dioxygenase activity (Pfam accession number PF03171), which can act on a variety of substrates (Schofield and Zhang, 1999; Costas et al., 2004). The catalytically active site is formed by a mononuclear non-haem Fe centre co-ordinated by two histidine residues and one carboxylate moiety (Hegg and Que, 1997; Zhou et al., 1998; Neidig et al., 2004; Purpero and Moran, 2007). We identified four active-site residues, His308, His356, Asp310, and Arg376, in the conserved 2OG-FeII_Oxy domain of BrAOP2.1 using the PROSITE database (http://prosite.expasy.org/) (Fig. 7).


Three genes encoding AOP2, a protein involved in aliphatic glucosinolate biosynthesis, are differentially expressed in Brassica rapa.

Zhang J, Liu Z, Liang J, Wu J, Cheng F, Wang X - J. Exp. Bot. (2015)

Four active-site residues identified in three BrAOP2 2OG-FeII_Oxy domains. The tertiary structure of each BrAOP2 protein was predicted with the program SWISS-MODEL, and the representation was made with Swiss Pdb-Viewer 4.01 (Arnold et al, 2006). (This figure is available in colour at JXB online.)
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4588880&req=5

Figure 7: Four active-site residues identified in three BrAOP2 2OG-FeII_Oxy domains. The tertiary structure of each BrAOP2 protein was predicted with the program SWISS-MODEL, and the representation was made with Swiss Pdb-Viewer 4.01 (Arnold et al, 2006). (This figure is available in colour at JXB online.)
Mentions: The two conserved domains DIOX-N and 2OG-FeII_Oxy at the N- and C-terminal regions of BrAOP2 (Fig. 2) are essential for 2-oxoglutarate/Fe(II)-dependent dioxygenase activity (Pfam accession number PF03171), which can act on a variety of substrates (Schofield and Zhang, 1999; Costas et al., 2004). The catalytically active site is formed by a mononuclear non-haem Fe centre co-ordinated by two histidine residues and one carboxylate moiety (Hegg and Que, 1997; Zhou et al., 1998; Neidig et al., 2004; Purpero and Moran, 2007). We identified four active-site residues, His308, His356, Asp310, and Arg376, in the conserved 2OG-FeII_Oxy domain of BrAOP2.1 using the PROSITE database (http://prosite.expasy.org/) (Fig. 7).

Bottom Line: Site-directed mutagenesis showed that His356, Asp310, and Arg376 residues are required for the catalytic activity of one of the BrAOP2 proteins (BrAOP2.1).Promoter-β-glucuronidase lines revealed that the BrAOP2.3 gene displayed an overlapping but distinct tissue- and cell-specific expression profile compared with that of the BrAOP2.1 and BrAOP2.2 genes.Taken together, our results revealed that all three BrAOP2 paralogues are active in B. rapa but have functionally diverged.

View Article: PubMed Central - PubMed

Affiliation: Institute of Vegetables and Flowers, Chinese Academy of Agricultural Sciences, Zhongguancun Nandajie No. 12, Haidian District, Beijing 100081, PR China.

No MeSH data available.