Journal
BMC PLANT BIOLOGY
Volume 21, Issue 1, Pages -Publisher
BMC
DOI: 10.1186/s12870-021-03220-1
Keywords
Anthocyanin degradation; PbLAC4-like; PbMYB26; Pear
Categories
Funding
- National Natural Science Foundation of China [31972372, 31572086, 31401845]
- China Agriculture Research System [CARS 28-45]
Ask authors/readers for more resources
The study found that the laccase encoded by PbLAC4-like in pear is associated with the degradation of anthocyanin. The expression pattern of PbLAC4-like is negatively correlated with anthocyanin content during the color fading process in different pear tissues. Overall, PbLAC4-like activated by PbMYB26 plays a crucial role in anthocyanin degradation, leading to red fading in pear tissues.
Background Decrease in anthocyanin content results in the loss of red color in leaves, petals and receptacles during development. The content of anthocyanin was affected by the biosynthesis and degradation of anthocyanin. Compared with the known detailed mechanism of anthocyanin biosynthesis, the degradation mechanism is not fully investigated. It is vital to study the degradation mechanism of anthocyanin in pear for promoting the accumulation of anthocyanin and inhibiting the red fading in pear. Results Here, we reported that laccase encoded by PbLAC4-like was associated with anthocyanin degradation in pear. The expression pattern of PbLAC4-like was negatively correlated with the content of anthocyanin during the color fading process of pear leaves, petals and receptacles. Phylogenetic analysis and sequence alignment revealed that PbLAC4-like played a vital role in anthocyanin degradation. Thus, the degradation of anthocyanin induced by PbLAC4-like was further verified by transient assays and prokaryotic expression. More than 80% of anthocyanin compounds were degraded by transiently over-expressed PbLAC4-like in pear fruitlet peel. The activity of crude enzyme to degrade anthocyanin in leaves at different stages was basically consistent with the expression of PbLAC4-like. The anthocyanin degradation ability of prokaryotic induced PbLAC4-like protein was also verified by enzyme activity assay. Besides, we also identified PbMYB26 as a positive regulator of PbLAC4-like. Yeast one-hybrid and dual luciferase assay results showed that PbMYB26 activated PbLAC4-like expression by directly binding to the PbLAC4-like promoter. Conclusions Taken together, the PbLAC4-like activated by PbMYB26, was involved in the degradation of anthocyanin, resulting in the redness fading in different pear tissues.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available