Abstract

BackgroundAcyl-CoA-binding proteins (ACBPs) are mainly involved in acyl-CoA ester binding and trafficking in eukaryotic cells, and their various functions have been characterized in model plants, such as Arabidopsis thaliana (A. thaliana), Oryza sativa (rice), and other plant species. In the present study, genome-wide mining and expression analysis of ACBP genes was performed on Hevea brasiliensis (the para rubber tree), the most important latex-producing crop in the world.ResultsSix members of the H. brasiliensis ACBP family genes, designated HbACBP1-HbACBP6, were identified from the H. brasiliensis genome. They can be categorized into four classes with different amino acid sequences and domain structures based on the categorization of their A. thaliana counterparts. Phylogenetic analysis shows that the HbACBPs were clustered with those of other closely related species, such as Manihot esculenta, Ricinus communis, and Jatropha carcas, but were further from those of A. thaliana, a distantly related species. Expression analysis demonstrated that the HbACBP1 and HbACBP2 genes are more prominently expressed in H. brasiliensis latex, and their expression can be significantly enhanced by bark tapping (a mechanical wound) and jasmonic acid stimulation, whereas HbACBP3-HbACBP6 had almost the same expression patterns with relatively high levels in mature leaves and male flowers, but a markedly low abundance in the latex. HbACBP1 and HbACBP2 may have crucial roles in lipid and latex metabolism in laticifers, so their subcellular location was further investigated and the results indicated that HbACBP1 is a cytosol protein, whereas HbACBP2 is an endoplasmic reticulum-associated ACBP.ConclusionsIn this study, the H. brasiliensis ACBP family genes were identified. Phylogenetic analyses of the HbABCPs indicate that there is a high conservation and evolutionary relationship between ACBPs in land plants. The HbACBPs are organ/tissue-specifically expressed and have different expression patterns in response to stimulation by bark tapping or ethrel/jasmonic acid. HbACBP1 and HbACBP2 are two important latex ACBPs that might be involved in the lipid and latex metabolism. The results may provide valuable information for further investigations into the biological functions of HbACBPs during latex metabolism and stress responses in H. brasiliensis.

Highlights

  • Acyl-CoA-binding proteins (ACBPs) are mainly involved in acyl-CoA ester binding and trafficking in eukaryotic cells, and their various functions have been characterized in model plants, such as Arabidopsis thaliana (A. thaliana), Oryza sativa, and other plant species

  • The H. brasiliensis ACBP family A total of six ACBP family genes were identified in the H. brasiliensis genome, and were designated as HbACBP1-HbACBP6, which were similar to those of the model plants A. thaliana and rice

  • Class I H. brasiliensis ACBP contained only one member, HbACBP1 with 92 amino acids, which is similar to A. thaliana ACBP6 (AtACBP6), and class II had only one member, i.e., HbACBP2 with 285 amino acids that consist of an ACB domain and ankyrin repeats

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Summary

Introduction

Acyl-CoA-binding proteins (ACBPs) are mainly involved in acyl-CoA ester binding and trafficking in eukaryotic cells, and their various functions have been characterized in model plants, such as Arabidopsis thaliana (A. thaliana), Oryza sativa (rice), and other plant species. The comprehensively characterized ACBP contains only about 90 amino acids (with an approximate molecular weight of 10 kDa), which is highly conserved and found in all four eukaryotic kingdoms and in some eubacterial species [6]. Plant ACBPs have been investigated in the model plants Arabidopsis thaliana (A. thaliana) and Oryza sativa (rice) [7, 8], and more ACBP genes have recently been characterized after genome sequencing other plant species e.g. Brassica napus [9], and the tung tree (Vernicia fordii) [10]. Classes I and III possess only one ACBD, class II contains one ACBD plus ankyrin repeats, and class IV contains one ACBD plus kelch motifs [11]

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