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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.


Multiple alignments of the BrAOP2, BoAOP2, and AtAOP2 protein sequences. Multiple alignments were performed using MEGA v.6.0. AtAOP2 is a known functional protein from Arabidopsis thaliana (ecotype Cvi), and BoAOP2 is from B. oleracea (collard). The solid lines above the alignment indicate the consensus sequences for the DIOX-N and 2OG-FeII_Oxy domains identified using the Conserved Domain Database (Marchler-Bauer et al., 2011)). The black shading indicates that at least four proteins share the same amino acid site. Asterisks show four active-site residues in the 2OG-FeII_Oxy domain.
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Figure 2: Multiple alignments of the BrAOP2, BoAOP2, and AtAOP2 protein sequences. Multiple alignments were performed using MEGA v.6.0. AtAOP2 is a known functional protein from Arabidopsis thaliana (ecotype Cvi), and BoAOP2 is from B. oleracea (collard). The solid lines above the alignment indicate the consensus sequences for the DIOX-N and 2OG-FeII_Oxy domains identified using the Conserved Domain Database (Marchler-Bauer et al., 2011)). The black shading indicates that at least four proteins share the same amino acid site. Asterisks show four active-site residues in the 2OG-FeII_Oxy domain.

Mentions: Alignment of the amino acids confirmed the presence of two conserved domains, DIOX-N and 2OG-FeII_Oxy, at the N-terminal and C-terminal regions of the BrAOP2s, respectively (Fig. 2). These two conserved domains are known to be responsible for 2-oxoglutarate/Fe(II)-dependent dioxygenase activity, which is associated with an important class of enzymes that mediate a variety of oxidative reactions (Prescott and Lloyd, 2000). In contrast to the two highly conserved domains, the middle part of BrAOP2 proteins only showed patches of similarity (Fig. 2). In this variable region, the deduced BrAOP2 proteins were all composed of three motifs (e.g. motif 12, 13, 14), with one additional motif 14 involved in BrAOP2.2 and BrAOP2.3, respectively (Supplementary Fig. S1 and Table S7, available at JXB online). The structural divergence of BrAOP2 proteins might have consequences for their functional diversification.


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)

Multiple alignments of the BrAOP2, BoAOP2, and AtAOP2 protein sequences. Multiple alignments were performed using MEGA v.6.0. AtAOP2 is a known functional protein from Arabidopsis thaliana (ecotype Cvi), and BoAOP2 is from B. oleracea (collard). The solid lines above the alignment indicate the consensus sequences for the DIOX-N and 2OG-FeII_Oxy domains identified using the Conserved Domain Database (Marchler-Bauer et al., 2011)). The black shading indicates that at least four proteins share the same amino acid site. Asterisks show four active-site residues in the 2OG-FeII_Oxy domain.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

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

Figure 2: Multiple alignments of the BrAOP2, BoAOP2, and AtAOP2 protein sequences. Multiple alignments were performed using MEGA v.6.0. AtAOP2 is a known functional protein from Arabidopsis thaliana (ecotype Cvi), and BoAOP2 is from B. oleracea (collard). The solid lines above the alignment indicate the consensus sequences for the DIOX-N and 2OG-FeII_Oxy domains identified using the Conserved Domain Database (Marchler-Bauer et al., 2011)). The black shading indicates that at least four proteins share the same amino acid site. Asterisks show four active-site residues in the 2OG-FeII_Oxy domain.
Mentions: Alignment of the amino acids confirmed the presence of two conserved domains, DIOX-N and 2OG-FeII_Oxy, at the N-terminal and C-terminal regions of the BrAOP2s, respectively (Fig. 2). These two conserved domains are known to be responsible for 2-oxoglutarate/Fe(II)-dependent dioxygenase activity, which is associated with an important class of enzymes that mediate a variety of oxidative reactions (Prescott and Lloyd, 2000). In contrast to the two highly conserved domains, the middle part of BrAOP2 proteins only showed patches of similarity (Fig. 2). In this variable region, the deduced BrAOP2 proteins were all composed of three motifs (e.g. motif 12, 13, 14), with one additional motif 14 involved in BrAOP2.2 and BrAOP2.3, respectively (Supplementary Fig. S1 and Table S7, available at JXB online). The structural divergence of BrAOP2 proteins might have consequences for their functional diversification.

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.