The effects of PhACL silencing on protein acetylation in petunia the effects of acetyl-CoA

ABSTRACT: Acetyl-coenzyme A (acetyl-CoA) is a central metabolite and the acetyl source for protein acetylation. The formation of cytosolic acetyl-CoA is catalyzed by ATP-citrate lyase (ACL) from citrate. However, the effects of acetyl-CoA on protein acetylation were not well known. In this study, four genes, PhACLA1, PhACLA2, PhACLB1, PhACLB2, encoding ACLA and ACLB submits in petunia (Petunia hybrida) were identified. VIGS-mediated PhACLA1-A2 and PhACLB1-B2 silencing leads to abnormal leave and flower development and reduced total anthocyanins content, while silencing of any single PhACL gene did not result in visible phenotype change. We quantitatively investigated the petunia proteome, acetylome, and the association between them in petunia corollas treated with pTRV2-PhACLB1-B2 and pTRV2. In total, 6200 protein groups were identified from petunia, among which 5343 proteins were quantified. A total of 345 proteins were up-regulated and 182 proteins were down-regulated (with a threshold of 1.2-fold) in PhACLB1-B2-silenced plant compared with the control (P <0.05). A total of 2210 lysine acetylation sites in 1148 protein groups were identified, among which 1744 sites in 921 proteins were accurately quantified (Additional file 2: Table S7). We subsequently used the quantification results of the global proteome to normalize the acetylome quantification data. From these, 68 sites in 54 lysine acetylation proteins were quantified as up-regulated targets and 40 sites in 38 lysine acetylation proteins were quantified as down-regulated targets at a threshold of 1.2 (P < 0.05). The global proteome and acetylome were negatively correlated, implying that proteome expression levels were negatively regulated by acetylation in PhACLB1-B2-silenced plants compared with the control.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Petunia Hybrida (petunia)

TISSUE(S): Corolla

SUBMITTER: Yixun Yu  

LAB HEAD: Yixun Yu

PROVIDER: PXD015480 | Pride | 2020-06-24

REPOSITORIES: Pride