Abstract
The protein phosphatase 2As (PP2As) play a key role in manipulating protein phosphorylation. Although a number of proteins in the latex of laticifers are phosphorylated during latex regeneration in rubber tree, information about the PP2A family is limited. In the present study, 36 members of the HbPP2A family were genome-wide identified. They were clustered into five subgroups: the subgroup HbPP2AA (4), HbPP2AB' (14), HbPP2AB'' (6), HbPP2AB55 (4), and HbPP2AC (8). The members within the same subgroup shared highly conserved gene structures and protein motifs. Most of HbPP2As possessed ethylene- and wounding-responsive cis-acting elements. The transcripts of 29 genes could be detected in latex by using published high-throughput sequencing data. Of the 29 genes, seventeen genes were significantly down-regulated while HbPP2AA1-1 and HbPP2AB55α/Bα-1were up-regulated by tapping. Of the 17 genes, 14 genes were further significantly down-regulated by ethrel application. The down-regulated expression of a large number of HbPP2As may attribute to the enhanced phosphorylation of the proteins in latex from the tapped trees and the trees treated with ethrel application.
Highlights
Protein phosphatase 2A (PP2A), a class of protein serine/threonine phosphatases, play a key role in manipulating protein phosphorylation by removing phosphate groups from the modified proteins [1,2]
Three AtPP2AA, nine AtPP2AB’, six AtPP2AB’’, two AtPP2AB55, and five AtPP2AC genes were used as queries to perform genome-wide identification of the HbPP2A family in rubber tree based on tBLASTn searches (E
The length of the HbPP2A proteins ranged from 280 aa (HbPP2AC6) to 588 aa (HbPP2AA1-1 and HbPP2AA2), the molecular weights ranged from 31.56 kDa (HbPP2AC6) to 65.57 kDa (HbPP2AA2), and their predicted isoelectric points ranged from 4.79 (HbPP2AC2-2) to 8.81 (HbPP2AB’η-5) (Table 1)
Summary
Protein phosphatase 2A (PP2A), a class of protein serine/threonine phosphatases, play a key role in manipulating protein phosphorylation by removing phosphate groups from the modified proteins [1,2]. The subunit A comprises a series of conserved alpha-helical repeats, providing a scaffold for the binding of B and C; the subunit B determines substrate specificity; the subunit C dimerizes with A to form an active conformation and serves as a platform for interactions with B [5]. Based on their structural characteristics, the B subunits are further classified into B, B0, and B@ [6]. Overexpression of StPP2Ac2b in Solanum tuberosum shows higher tuber induction rates compared
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