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.


Functional complementation analyses of BrAOP2 genes in Arabidopsis thaliana Col-0. The glucosinolate content and profile were determined in 6-week-old rosette leaves. Three independent mutant-complemented lines for each BrAOP2 gene were analysed, and average foliar glucosinolates from 30 individual plants are represented along with their standard errors. Asterisks indicate significant differences in glucosinolate content compared with Col-0 (P<0.05, one-way ANOVA analysis with a Duncan post-hoc test). PRO, 2-hydroxy-3-butenyl-glucosinolate; SIN, sinigrin.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

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

Figure 6: Functional complementation analyses of BrAOP2 genes in Arabidopsis thaliana Col-0. The glucosinolate content and profile were determined in 6-week-old rosette leaves. Three independent mutant-complemented lines for each BrAOP2 gene were analysed, and average foliar glucosinolates from 30 individual plants are represented along with their standard errors. Asterisks indicate significant differences in glucosinolate content compared with Col-0 (P<0.05, one-way ANOVA analysis with a Duncan post-hoc test). PRO, 2-hydroxy-3-butenyl-glucosinolate; SIN, sinigrin.

Mentions: The functional complementation among the BrAOP2 genes catalysed the conversion of the C3 and C4 methylsulfinylalkyl glucosinolate to alkenyl glucosinolates (e.g. sinigrin and NAP); this conversion was not observed in the Col-0 control (Fig. 6). Line BrAOP2.3-14-2 showed a high level of conversion of the precursor methylsulfinylalkyl glucosinolate to sinigrin and NAP as well as to 2-hydroxy-3-butenyl-glucosinolate (PRO). PRO was further hydroxylated by the action of the GS-OH locus product (Mithen et al., 1995). The two lines BrAOP2.1-15-5 and BrAOP2.1-18-8 both showed a slightly lower conversion of the precursor methylsulfinylalkyl glucosinolate to sinigrin and NAP. All three BrAOP2.2 lines showed relatively low conversions of the precursor methylsulfinylalkyl glucosinolate to sinigrin and NAP, producing trace amounts of PRO. Thus, the mutant complementation analysis in Arabidopsis thaliana clearly suggested that all three BrAOP2 genes had biological activities in vivo.


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)

Functional complementation analyses of BrAOP2 genes in Arabidopsis thaliana Col-0. The glucosinolate content and profile were determined in 6-week-old rosette leaves. Three independent mutant-complemented lines for each BrAOP2 gene were analysed, and average foliar glucosinolates from 30 individual plants are represented along with their standard errors. Asterisks indicate significant differences in glucosinolate content compared with Col-0 (P<0.05, one-way ANOVA analysis with a Duncan post-hoc test). PRO, 2-hydroxy-3-butenyl-glucosinolate; SIN, sinigrin.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

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

Figure 6: Functional complementation analyses of BrAOP2 genes in Arabidopsis thaliana Col-0. The glucosinolate content and profile were determined in 6-week-old rosette leaves. Three independent mutant-complemented lines for each BrAOP2 gene were analysed, and average foliar glucosinolates from 30 individual plants are represented along with their standard errors. Asterisks indicate significant differences in glucosinolate content compared with Col-0 (P<0.05, one-way ANOVA analysis with a Duncan post-hoc test). PRO, 2-hydroxy-3-butenyl-glucosinolate; SIN, sinigrin.
Mentions: The functional complementation among the BrAOP2 genes catalysed the conversion of the C3 and C4 methylsulfinylalkyl glucosinolate to alkenyl glucosinolates (e.g. sinigrin and NAP); this conversion was not observed in the Col-0 control (Fig. 6). Line BrAOP2.3-14-2 showed a high level of conversion of the precursor methylsulfinylalkyl glucosinolate to sinigrin and NAP as well as to 2-hydroxy-3-butenyl-glucosinolate (PRO). PRO was further hydroxylated by the action of the GS-OH locus product (Mithen et al., 1995). The two lines BrAOP2.1-15-5 and BrAOP2.1-18-8 both showed a slightly lower conversion of the precursor methylsulfinylalkyl glucosinolate to sinigrin and NAP. All three BrAOP2.2 lines showed relatively low conversions of the precursor methylsulfinylalkyl glucosinolate to sinigrin and NAP, producing trace amounts of PRO. Thus, the mutant complementation analysis in Arabidopsis thaliana clearly suggested that all three BrAOP2 genes had biological activities in vivo.

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.