Acyl-CoA-binding protein (ACBP)

  • 文章类型: Journal Article
    背景:酰基辅酶A结合蛋白(ACBP)作为辅酶A转运蛋白,在调节植物生长和发育以应对非生物胁迫和植物激素方面发挥重要作用,以及在膜修复。迄今为止,ACBP家族在大麦(大麦)中尚未得到全面表征。
    结果:在大麦基因组中鉴定出8个ACBP基因,命名为HvACBP1-8。对HvACBP的蛋白质结构和启动子元件的分析表明其在植物生长中的潜在功能。发展,和应激反应。这些HvACBPs在非生物胁迫如干旱诱导后,在特定的组织和器官中表达。盐度,UV-B暴露,极端温度,和暴露于外源植物激素。HvACBP7和HvACBP8氨基酸序列在西藏青克大麦驯化过程中保守。
    结论:酰基辅酶A结合蛋白可能在大麦生长和环境适应中起重要作用。本研究为进一步分析HvACBPs在大麦应激反应中的生物学功能奠定了基础。
    BACKGROUND: Acyl-CoA-Binding proteins (ACBPs) function as coenzyme A transporters and play important roles in regulating plant growth and development in response to abiotic stress and phytohormones, as well as in membrane repair. To date, the ACBP family has not been a comprehensively characterized in barley (Hordeum vulgare L.).
    RESULTS: Eight ACBP genes were identified in the barley genome and named as HvACBP1-8. The analysis of the proteins structure and promoter elements of HvACBP suggested its potential functions in plant growth, development, and stress response. These HvACBPs are expressed in specific tissues and organs following induction by abiotic stressors such as drought, salinity, UV-B exposure, temperature extremes, and exposure to exogenous phytohormones. The HvACBP7 and HvACBP8 amino acid sequences were conserved during the domestication of Tibetan Qingke barley.
    CONCLUSIONS: Acyl-CoA-binding proteins may play important roles in barley growth and environmental adaptation. This study provides foundation for further analyses of the biological functions of HvACBPs in the barley stress response.
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  • 文章类型: Journal Article
    在所有被调查的真核生物中发现,酰基辅酶A结合蛋白(ACBP)通过以高亲和力特异性结合酰基辅酶A酯参与脂质代谢。ACBP家族蛋白的结构和功能已经在酵母中得到了广泛的描述,真菌,植物和哺乳动物,但不是卵菌.在本研究中,从大豆疫霉基因组中鉴定出7个ACBP基因PsACBP1-7,大豆的卵菌病原体。创建靶向PsACBP1和PsACBP2的CRISPR-Cas9敲除突变体用于表型测定。PsACBP1敲除导致孢子囊产生和毒力缺陷。PsACBP2敲除突变体表现出受损的营养生长,动物园孢子生产,囊肿萌发和毒力。此外,PsACBP2敲除和过表达系的尼罗红染色表明,PsACBP2参与了大豆假单胞菌的脂质形成。我们的结果表明,两个ACBP基因的生长和发育所需的不同,两者都对大豆的毒力至关重要。
    Being found in all eukaryotes investigated, acyl-CoA-binding proteins (ACBPs) participate in lipid metabolism via specifically binding acyl-CoA esters with high affinity. The structures and functions of ACBP family proteins have been extensively described in yeasts, fungi, plants and mammals, but not oomycetes. In the present study, seven ACBP genes named PsACBP1-7 were identified from the genome of Phytophthora sojae, an oomycete pathogen of soybean. CRISPR-Cas9 knockout mutants targeting PsACBP1 and PsACBP2 were created for phenotypic assays. PsACBP1 knockout led to defects in sporangia production and virulence. PsACBP2 knockout mutants exhibited impaired vegetative growth, zoospore production, cyst germination and virulence. Moreover, Nile red staining of PsACBP2 knockout and over-expression lines showed that PsACBP2 is involved in the formation of lipid bodies in P. sojae. Our results demonstrate that two ACBP genes are differently required for growth and development, and both are essential for virulence in P. sojae.
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  • 文章类型: Journal Article
    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. 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.
    Six 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.
    In 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.
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  • 文章类型: Journal Article
    Adipokinetic hormone (AKH) has been associated with the control of energy metabolism in a large number of arthropod species due to its role on the stimulation of lipid, carbohydrate and amino acid mobilization/release. In the insect Rhodnius prolixus, a vector of Chagas\' disease, triacylglycerol (TAG) stores must be mobilized to sustain the metabolic requirements during moments of exercise or starvation. Besides the recent identification of the R. prolixus AKH peptide, other components required for the AKH signaling cascade and its mode of action remain uncharacterized in this insect. In the present study, we identified and investigated the expression profile of the gene encoding the AKH receptor of R. prolixus (RhoprAkhr). This gene is highly conserved in comparison to other sequences already described and its transcript is abundant in the fat body and the flight muscle of the kissing bug. Moreover, RhoprAkhr expression is induced in the fat body at moments of increased TAG mobilization; the knockdown of this gene resulted in TAG accumulation both in fat body and flight muscle after starvation. The inhibition of Rhopr-AKHR transcription as well as the treatment of insects with the peptide Rhopr-AKH in its synthetic form altered the transcript levels of two genes involved in lipid metabolism, the acyl-CoA-binding protein-1 (RhoprAcbp1) and the mitochondrial glycerol-3-phosphate acyltransferase-1 (RhoprGpat1). These results indicate that the AKH receptor is regulated at transcriptional level and is required for TAG mobilization under starvation. In addition to the classical view of AKH as a direct regulator of enzymatic activity, we propose here that AKH signaling may account for the regulation of nutrient metabolism by affecting the expression profile of target genes.
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  • 文章类型: Journal Article
    酰基-CoA结合蛋白(ACBP)显示在酰基-CoA结合(ACB)结构域处的保守性,其促进与酰基-CoA酯的结合。在拟南芥中,六个ACBP参与发育和应激反应。水稻(Oryzasativa)也包含六个编码ACBPs的基因。我们调查了单子叶水稻和大青菜ACBP之间亚细胞定位的差异。通过绿色荧光蛋白(GFP)融合体在烟草(Nicotianatabacum)表皮细胞中的瞬时表达,实现了六个OsACBP的亚细胞定位。和拟南芥的稳定转化。由于过氧化物酶体中没有植物ACBP的报道,通过在水稻鞘细胞中的瞬时表达证实了OsACBP6::GFP定位。通过在过氧化物酶体abc转运蛋白1(pxa1)突变体中过表达35S::OsACBP6,研究了OsACBP6的功能,该突变体在过氧化物酶体脂肪酸β-氧化中存在缺陷。正如预测的那样,OsACBP1::GFP和OsACBP2::GFP定位于胞质溶胶,和OsACBP4::GFP和OsACBP5::GFP到达内质网(ER)。然而,OsACBP3::GFP显示亚细胞多定位,而OsACBP6::GFP定位于过氧化物酶体。35S::OsACBP6-OE/pxa1系显示吲哚-3-丁酸(IBA)过氧化物酶体β-氧化的恢复,创伤诱导的营养储存蛋白1(VSP1)表达和茉莉酸(JA)积累。这些发现表明OsACBP6在过氧化物酶体β-氧化中的作用,并表明水稻ACBPs除了参与脂质生物合成外,还参与脂质降解。
    Acyl-CoA-binding proteins (ACBPs) show conservation at the acyl-CoA-binding (ACB) domain which facilitates binding to acyl-CoA esters. In Arabidopsis thaliana, six ACBPs participate in development and stress responses. Rice (Oryza sativa) also contains six genes encoding ACBPs. We investigated differences in subcellular localization between monocot rice and eudicot A. thaliana ACBPs. The subcellular localization of the six OsACBPs was achieved via transient expression of green fluorescence protein (GFP) fusions in tobacco (Nicotiana tabacum) epidermal cells, and stable transformation of A. thaliana. As plant ACBPs had not been reported in the peroxisomes, OsACBP6::GFP localization was confirmed by transient expression in rice sheath cells. The function of OsACBP6 was investigated by overexpressing 35S::OsACBP6 in the peroxisomal abc transporter1 (pxa1) mutant defective in peroxisomal fatty acid β-oxidation. As predicted, OsACBP1::GFP and OsACBP2::GFP were localized to the cytosol, and OsACBP4::GFP and OsACBP5::GFP to the endoplasmic reticulum (ER). However, OsACBP3::GFP displayed subcellular multi-localization while OsACBP6::GFP was localized to the peroxisomes. 35S::OsACBP6-OE/pxa1 lines showed recovery in indole-3-butyric acid (IBA) peroxisomal β-oxidation, wound-induced VEGETATIVE STORAGE PROTEIN1 (VSP1) expression and jasmonic acid (JA) accumulation. These findings indicate a role for OsACBP6 in peroxisomal β-oxidation, and suggest that rice ACBPs are involved in lipid degradation in addition to lipid biosynthesis.
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