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Arabidopsis thaliana Acyl-CoA-binding protein ACBP6 interacts with plasmodesmata-located protein PDLP8.

ABSTRACT: In Arabidopsis thaliana, six acyl-CoA-binding proteins (ACBPs), designated as AtACBP1 to AtACBP6, have been identified to function in various events related to plant stress and development. The 10-kDa AtACBP6 is the smallest in this protein family, and recombinant AtACBP6 interacts with lipids in vitro by binding to acyl-CoA esters and phosphatidylcholine. Using anti-AtACBP6 antibodies in immunoelectron microscopy, we have localized AtACBP6 in the Arabidopsis phloem. The detection of immunogold grains in the plasmodesmata suggested that AtACBP6 could move from the companion cells to the sieve elements via the plasmodesmata. As AtACBP6 has been identified in a membrane-based interactome analysis to be a potential protein partner of Plasmodesmata-Localized Protein, PDLP8, AtACBP6-PDLP8 interaction was investigated herein utilizing isothermal titration calorimetry, as well as pull-down and bimolecular fluorescence complementation assays (BiFC). Notably, BiFC data revealed that AtACBP6-PDLP8 interaction occurred at the plasma membrane, which was unexpected as AtACBP6 has been previously identified in the cytosol. AtACBP6 expression was generally higher than PDLP8 in ?-glucuronidase (GUS) assays on transgenic Arabidopsis transformed with AtACBP6 or PDLP8 promoter-driven GUS, consistent with qRT-PCR and microarray results. Furthermore, western blot analysis using anti-AtACBP6 antibodies showed a reduction in AtACBP6 expression in the pdlp8 T-DNA insertional mutant, suggesting that PDLP8 may possibly influence AtACBP6 accumulation in the sieve elements, probably in the plasmodesmata, where PDLP8 is confined and to where AtACBP6 has been immunodetected.

SUBMITTER: Ye ZW

PROVIDER: S-EPMC5616145 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature

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Arabidopsis thaliana Acyl-CoA-binding protein ACBP6 interacts with plasmodesmata-located protein PDLP8.

Ye Zi-Wei ZW Chen Qin-Fang QF Chye Mee-Len ML

Plant signaling & behavior 20170808 8

In Arabidopsis thaliana, six acyl-CoA-binding proteins (ACBPs), designated as AtACBP1 to AtACBP6, have been identified to function in various events related to plant stress and development. The 10-kDa AtACBP6 is the smallest in this protein family, and recombinant AtACBP6 interacts with lipids in vitro by binding to acyl-CoA esters and phosphatidylcholine. Using anti-AtACBP6 antibodies in immunoelectron microscopy, we have localized AtACBP6 in the Arabidopsis phloem. The detection of immunogold ...[more]

PMID: 28786767

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Project description:As plant seed oils provide animals with essential fatty acids (FAs), genes that regulate plant lipid metabolism have been used in genetic manipulation to improve dietary seed oil composition and benefit human health. Herein, the Arabidopsis thaliana cytosolic acyl-CoA-binding proteins (AtACBPs), AtACBP4, AtACBP5, and AtACBP6 were shown to play a role in determining seed oil content by analysis of atacbp (atacbp4, atacbp5, atacbp6, atacbp4atacbp5, atacbp4atacbp6, atacbp5atacbp6, and atacbp4atacbp5atacbp6) seed oil content in comparison with the Col-0 wild type (WT). Triacylglycerol (TAG) composition in electrospray ionization-mass spectrometer (ESI-MS) analysis on atacbp6 seed oil showed a reduction (-50%) of C58-TAGs in comparison with the WT. Investigations on fatty acid composition of atacbp mutants indicated that 18:2-FA accumulated in atacbp6 and 18:3-FA in atacbp4, both at the expense of 20:1-FA. As TAG composition can be modified by acyl editing through phosphatidylcholines (PC) and lysophosphatidylcholines (LPC), total PC and LPC content in atacbp6 mature seeds was determined and ESI-MS analysis revealed that LPC had increased (+300%) at the expense of PC. Among all the 14 tested PC species, all (34:1-, 34:2-, 34:3-, 34:4-, 34:5-, 34:6-, 36:2-, 36:3-, 36:5-, 36:6-, 38:2-, 38:3-, and 38:4-PCs) but 36:4-PC were lower in atacbp6 than the WT. In contrast, all LPC species (16:0-, 18:1-, 18:2-, 18:3-, and 20:1-LPC) examined were elevated in atacbp6. LPC abundance also increased in atacbp4atacbp5, but not atacbp4 and atacbp5. Interestingly, when LPC composition in atacbp4atacbp5 was compared with atacbp4 and atacbp5, significant differences were observed between atacbp4atacbp5 and each single mutant, implying that AtACBP4 and AtACBP5 play combinatory roles by affecting LPC (but not PC) biosynthesis. Furthermore, PC-related genes such as those encoding acyl-CoA:lysophphosphatidylcholine acyltransferase (LPCAT1) and phospholipase A2 alpha (PLA2α) were upregulated in atacbp6 developing seeds. A model on the role of AtACBP6 in modulating TAG through regulating LPCAT1 and PLA2α expression is proposed. Taken together, cytosolic AtACBPs appear to affect unsaturated TAG content and are good candidates for engineering oil crops to enhance seed oil composition.

Dataset Information

Arabidopsis thaliana Acyl-CoA-binding protein ACBP6 interacts with plasmodesmata-located protein PDLP8.

Publications

Arabidopsis thaliana Acyl-CoA-binding protein ACBP6 interacts with plasmodesmata-located protein PDLP8.

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