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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.


Subcellular localization of BrAOP2 proteins in B. rapa protoplasts. Images were taken in a dark field for green fluorescence and chloroplast autofluorescence (red), while the outlook of cells was photographed in a bright field. Bar, 10 µm.
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Figure 4: Subcellular localization of BrAOP2 proteins in B. rapa protoplasts. Images were taken in a dark field for green fluorescence and chloroplast autofluorescence (red), while the outlook of cells was photographed in a bright field. Bar, 10 µm.

Mentions: To investigate the subcellular localization of the three BrAOP2 proteins, three ProCAMV35S:BrAOP2:GFP vectors were constructed and their localization was detected by monitoring the transient expression of GFP in B. rapa mesophyll protoplast cells (Fig. 4). A strong green fluorescent signal was observed in the cytoplasm of transiently transformed cells, demonstrating that the three BrAOP2 proteins were predominantly cytoplasmic, consistent with the subcellular localization for the secondary modification of aliphatic glucosinolates in Arabidopsis (Sonderby et al., 2010).


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)

Subcellular localization of BrAOP2 proteins in B. rapa protoplasts. Images were taken in a dark field for green fluorescence and chloroplast autofluorescence (red), while the outlook of cells was photographed in a bright field. Bar, 10 µm.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

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

Figure 4: Subcellular localization of BrAOP2 proteins in B. rapa protoplasts. Images were taken in a dark field for green fluorescence and chloroplast autofluorescence (red), while the outlook of cells was photographed in a bright field. Bar, 10 µm.
Mentions: To investigate the subcellular localization of the three BrAOP2 proteins, three ProCAMV35S:BrAOP2:GFP vectors were constructed and their localization was detected by monitoring the transient expression of GFP in B. rapa mesophyll protoplast cells (Fig. 4). A strong green fluorescent signal was observed in the cytoplasm of transiently transformed cells, demonstrating that the three BrAOP2 proteins were predominantly cytoplasmic, consistent with the subcellular localization for the secondary modification of aliphatic glucosinolates in Arabidopsis (Sonderby et al., 2010).

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.