磷缺失引起小麦叶片中脂含量的变化与脂的合成和磷脂酰甘油的降解有关(英文)

对生长在不同磷营养水平条件下小麦(Triticum aestivum var.Zhongyou 9507)叶片中光合膜脂含量变化的原因进行了研究。通过对生长在不同磷营养水平条件下9 d龄和16 d龄小麦叶片中光合膜脂含量的分析,发现在磷缺失培养条件下,小麦光合膜脂的相对含量发生了很大变化,这种变化与小麦叶龄密切相关。在16 d龄小麦植株中,第一片叶为老叶,第二片叶为较老叶,而第三片叶为新叶,PG和MGDG在叶片中的相对含量从新叶到老叶逐渐下降,而DGDG和SQDG含量逐渐上升;在磷缺失条件下,16 d龄小麦第一叶片中PG的含量(2.5％)远远低于其在9 d龄第一叶片中的含量(5.5％)。以上结果说明,磷缺失引起小麦叶片中脂含量的变化不仅与脂合成有关,而且与PG的降解有关;新生叶片中PG含量减少的主要原因是由于磷供应不足,从而影响了PG的合成;而PG的降解则是老叶中PG含量下降的主要原因。     

植物中草酸积累与光呼吸乙醇酸代谢的关系

对几种C3 和C4 植物中草酸含量及相应的乙醇酸氧化酶活性测定结果表明 :叶片光呼吸强度及其关键酶活性大小与草酸积累量没有相关性 ;植物根中均能积累草酸 ,但未测出乙醇酸氧化酶活性。烟草根、叶中的草酸含量在不同生长时期差异明显 ,且二者呈极显著正相关 (y =2 .5 6 5lnx 2 .137,r =0 .749,P <0 .0 0 1) ,说明根中草酸可能来自叶片。氧化乙醇酸的酶的活性与氧化乙醛酸的酶的活性呈极显著线性正相关 (y =0 .2 41x 0 .0 0 6 ,r=0 .96 7,P <0 .0 0 0 1) ,进一步证实是乙醇酸氧化酶催化了两种底物的反应。烟草在不同生长期叶片中草酸总含量变化与相应的乙醇酸氧化酶活性变化亦没有相关性 ;低磷胁迫可显著诱导烟草根叶中的草酸形成和分泌 ,但并未影响乙醇酸氧化酶活性 ,进一步证明草酸积累与该酶活性大小无关     

磷缺失引起小麦叶片中脂含量的变化与脂的合成和磷脂酰甘油的降解有关

对生长在不同磷营养水平条件下小麦(Triticum aestivum var.Zhongyou 9507)叶片中光合膜脂含量变化的原因进行了研究.通过对生长在不同磷营养水平条件下9 d龄和16 d龄小麦叶片中光合膜脂含量的分析,发现在磷缺失培养条件下,小麦光合膜脂的相对含量发生了很大变化,这种变化与小麦叶龄密切相关.在16d龄小麦植株中,第一片叶为老叶,第二片叶为较老叶,而第三片叶为新叶,PG和MGDG在叶片中的相对含量从新叶到老叶逐渐下降,而DGDG和SQDG含量逐渐上升;在磷缺失条件下,16 d龄小麦第一叶片中PG的含量(2.5%)远远低于其在9 d龄第一叶片中的含量(5.5%).以上结果说明,磷缺失引起小麦叶片中脂含量的变化不仅与脂合成有关,而且与PG的降解有关;新生叶片中PG含量减少的主要原因是由于磷供应不足,从而影响了PG的合成;而PG的降解则是老叶中PG含量下降的主要原因.     

水分胁迫对棉花叶片中IAA从含量、IAA氧化酶和过氧化物酶活性的影响

整株干旱降低盐棉46号叶片中的IAA总量,叶龄愈小下降愈多。幼叶中IAA总量的下降主要是结合态IAA减少的结果。气干和-1.7MPa PEG溶液渗透胁迫处理也降低离体成熟叶片的IAA总量,其变化与叶片含水量呈直线相关(r=0.905)。整株干旱处理提高各叶片的过氧化物酶活性,叶龄愈小提高愈多,但IAA氧化酶活性无显著变化。离体和整株干旱时IAA总量的下降,可能是过氧化物酶活性增加所致。     

缺磷胁迫下烟草中草酸含量的变化（简报）

用1／2Hoagland营养液培养6个不同烟草品种,于缺磷后不同时期,测定根、叶中草酸含量的结果显示,在处理后10d时的根和叶中草酸含量均开始上升,并随胁迫时间的延长而增大,其中以中烟90和牛津26提高最为显著。根中未测出乙醇酸氧化酶活化,叶中此酶的活性较高,但不受缺磷胁迫的影响;缺磷处理的根和叶中异柠檬酸裂解酶活性变化也不明显。     

拟南芥中H_2S与PLDα1响应干旱胁迫的作用研究

以野生型拟南芥WT、PLDα1合成缺陷突变体pldα1-1以及L-半胱氨酸脱巯基酶(L-cysteine desulfyrase,L-CDes)合成缺陷突变体lcd-4幼苗为材料,以0.3 mol·L~(-1)甘露醇模拟干旱胁迫,研究磷脂酶Dα1(phospholipase Dα1,PLDα1)与气体信号分子硫化氢(hydrogen sulfide,H2S)响应干旱胁迫的作用及可能存在的信号关系。结果显示:干旱胁迫下,野生型拟南芥的H_2S含量、PLD与L/D-CDes活性及其基因相对表达量均发生显著的变化。萌发率实验中,与WT相比,pldα1-1和lcd-4对干旱胁迫更加敏感,外施NaHS可以促进干旱胁迫下WT、pldα1-1以及lcd-4种子萌发及內源H_2S产生,而外施PA能提高干旱胁迫下WT、pldα1-1种子萌发率及H_2S含量,但对lcd-4萌发率及H_2S含量没有显著影响。研究结果表明,信号分子H_2S和PLDα1在拟南芥的干旱胁迫响应中发挥一定的作用,且H_2S可能位于PLDα1的下游参与调控拟南芥种子萌发的信号过程。     

外源胆固醇对水稻幼苗膜脂组成及抗冷力的影响

分析了水稻幼苗低温胁迫前后膜脂和膜脂脂肪酸含量变化。结果表明,经胆固醇处理的幼苗叶和根细胞膜脂中LPC、PS和PG含量比对照下降少,PA含量增加也较少。胆固醇处理的幼苗叶和根棕榈酸(16:0)增加量和亚麻酸(18:3)与IUFA减少量均明显比对照少。试验结果证明,水稻幼苗叶片和根系的抗冷力与PA含量和脂肪酸不饱和程度变化有密切关系。外源胆固醇处理水稻幼苗能阻止低温对膜脂的破坏作用,提高幼苗抗低温胁迫能力。     

驳枝对早花烟草成熟期间叶中叶绿素含量、硝酸还原酶和淀粉酶活性的影响

对早花烟草驳枝后,其成熟期间中部和上部叶中叶绿素（Ch1）含量和硝酸还原酶（NR）活性下降,下部叶则增高,成熟后期的上部叶中淀粉酶（AM）活性明显增强。经驳枝的烟草,中、上部叶烘烤后叶中淀粉、氮和烟碱含量下降,下部叶中的淀粉含量无明显变化。     

干旱胁迫下磷脂酶Dδ和9-脂氧合酶对拟南芥茉莉酸合成及种子萌发的影响

以拟南芥哥伦比亚野生型(WT)、磷脂酶Dδ(PLDδ)缺失型突变体pldδ和9-脂氧合酶(9-LOX)缺失型突变体lox1、lox5实生苗为材料,以0.3 mol·L-1甘露醇模拟干旱胁迫,分析PLDδ和9-LOX参与干旱胁迫下拟南芥茉莉酸(JA)生物合成和在种子萌发中作用。结果表明:干旱胁迫显著提高PLDδ和LOX1基因表达以及PLD和LOX酶活性;干旱胁迫下,pldδ突变体幼苗的LOX活性和JA含量显著低于WT,外源添加磷脂酸(PA)后LOX活性和JA含量显著上升,并高于WT;干旱胁迫显著抑制pldδ、lox1和lox5突变体的种子萌发,以对lox1的抑制效果最为明显;干旱胁迫下PLD活性上升与PLDδ基因表达上调有关,LOX活性上升与LOX1和LOX5基因表达上调有关,其中LOX1基因起主要作用;PLDδ/PA位于9-LOX上游参与9-LOX诱导的JA合成过程;PLDδ、LOX1和LOX5基因均参与干旱胁迫下拟南芥的种子萌发,LOX1在此过程中作用最为明显;PLDδ和9-LOX均参与PA和JA介导的种子萌发过程。     

烟草植株各部位的草酸含量变化（简报）

土培与水培的中烟90烟草植株中草酸含量呈现叶片与根中高,茎中低的哑铃状,根中含量高于叶片,根、,不同叶位叶片和不同部位茎中含量在在早晚没有明显差异。叶片中的含量随叶位不同而不同,成熟叶的含量高于幼叶和老叶。     

Distinct Ca2+ binding properties of novel C2 domains of plant phospholipase dalpha and beta

Of the isoforms of plant phospholipase D (PLD) that have been cloned and characterized, PLDalpha requires millimolar levels of Ca(2+) for optimal activity, whereas PLDbeta is most active at micromolar concentrations of Ca(2+). Multiple amino acid sequence alignments suggest that PLDalpha and PLDbeta both contain a Ca(2+)-dependent phospholipid-binding C2 domain near their N termini. In the present study, we expressed and characterized the putative C2 domains of PLDalpha and PLDbeta, designated PLDalpha C2 and PLDbeta C2, by CD spectroscopy, isothermal titration calorimetry, and phospholipid binding assay. Both PLD C2 domains displayed CD spectra consistent with anticipated major beta-sheet structures but underwent spectral changes upon binding Ca(2+); the magnitude was larger for PLDbeta C2. These conformational changes, not shown by any of the previously characterized C2 domains of animal origin, occurred at micromolar Ca(2+) concentrations for PLDbeta C2 but at millimolar levels of the cation for PLDalpha C2. PLDbeta C2 exhibited three Ca(2+)-binding sites: one with a dissociation constant (K(d)) of 0.8 microm and the other two with a K(d) of 24 micrometer. In contrast, isothermal titration calorimetry data of PLDalpha C2 were consistent with 1-3 low affinity Ca(2+)-binding sites with K(d) in the range of 590-470 micrometer. The thermodynamics of Ca(2+) binding markedly differed for the two C2 domains. Likewise, PLDbeta C2 bound phosphatidylcholine (PC), the substrate of PLD, in the presence of submillimolar Ca(2+) concentrations, whereas PLDalpha C2 did so only in the presence of millimolar levels of the metal ion. Both C2 domains bound phosphatidylinoistol 4,5-bisphosphate, a regulator of PC hydrolysis by PLD. However, added Ca(2+) displaced the bound phosphatidylinoistol 4,5-bisphosphate. Ca(2+) and PC binding properties of PLDalpha C2 and PLDbeta C2 follow a trend similar to the Ca(2+) requirements of the whole enzymes, PLDalpha and PLDbeta, for PC hydrolysis. Taken together, the results suggest that the C2 domains of PLDalpha and PLDbeta have novel structural features and serve as handles by which Ca(2+) differentially regulates the activities of the isoforms.     

In vivo substrates and the contribution of the common phospholipase D, PLDalpha, to wound-induced metabolism of lipids in Arabidopsis

The common plant phospholipase D (PLD), PLDalpha, has been proposed to be involved in wound-induced production of jasmonic acid. To better understand the role(s) of PLDalpha in the wound response, detailed lipid analysis was carried out to determine the in vivo substrates and the contribution of PLDalpha in wound-induced lipid metabolism in Arabidopsis thaliana. Mechanical wounding of Arabidopsis leaves resulted in significantly less hydrolysis of phosphatidylcholine (PC) in PLDalpha-deficient than in wild-type plants. Hydrolysis of phosphatidylethanolamine, phosphatidylglycerol (PG), and phosphatidylinositol within 30 min of wounding was not significantly different in PLDalpha-deficient and wild-type leaves. Phosphatidic acid (PA) levels increased rapidly in wild-type and, to a lesser extent, in PLDalpha-deficient plants. The acyl composition of the PA generated by wounding suggests that the major in vivo substrate of PLD in wild-type leaves was PC, and that PG hydrolysis accounted for 10-15% of the wound-induced PA in wild-type leaves. Comparison of the acyl compositions of the wound-induced PA of wild-type and PLDalpha-deficient leaves indicated that PLDalpha hydrolyzed PG more readily than other PLD isoforms did. Wounding produced substantial increases in free linoleic and linolenic acids in wild-type plants, whereas PLDalpha-deficient plants showed only a slight increase in linoleic acid and no significant increase in linolenic acid. These results demonstrate that PLDalpha and at least one other PLD isoform, as well as other hydrolytic enzymes, are active in mechanically wounded Arabidopsis leaves, and PLDalpha is involved in wound-induced metabolism of polyunsaturated fatty acids.     

Phosphatidylglycerol Degradation is One Crucial Reason for the Decrease of its Concentration in Wheat Leaves under Phosphate Deprivation Stress

Phosphatidylglycerol (PG) is of crucial importance for the organization and function of thylakoid membranes. The reason for a decrease of PG concentration in plants under phosphate deprivation stress still remains unclear. By comparing PG concentration and PG hydrolase activity of wheat leaves at different developmental stages, we show that when the first leaves are fully developed, the PG concentration and PG hydrolase activity in phosphate-deficient plants were similar to those of the controls. With age, there was a significant decrease in PG concentration combined with an increase in PG hydrolase activity for phosphate-deficient plants. The close correlation between the decrease in PG concentration and the increase in PG hydrolases activities suggests that PG hydrolysis was the most important factor responsible for the decrease in its concentration. The main hydrolysis products of PG are phosphatidic acid (PA), diacylglycerol (DAG) and free fatty acid (FFA). The application of an inhibitor, n-butanol, which blocks the formation of PA via the PLD pathway, to the in vitro enzyme reaction mixture may restrict PA and DAG production. Neomycin sulfate, a PLC inhibitor, was shown to exhibit significant inhibition in DAG generation. These results suggest that both PLD and PLC were responsible for PG degradation in the leaves of phosphate-deficient wheat. The possible role of PLA activity for PG degradation is also discussed.     

Involvement of phospholipase D in wound-induced accumulation of jasmonic acid in arabidopsis

Multiple forms of phospholipase D (PLD) were activated in response to wounding, and the expressions of PLDalpha, PLDbeta, and PLDgamma differed in wounded Arabidopsis leaves. Antisense abrogation of the common plant PLD, PLDalpha, decreased the wound induction of phosphatidic acid, jasmonic acid (JA), and a JA-regulated gene for vegetative storage protein. Examination of the genes involved in the initial steps of oxylipin synthesis revealed that abrogation of the PLDalpha attenuated the wound-induced expression of lipoxygenase 2 (LOX2) but had no effect on allene oxide synthase (AOS) or hydroperoxide lyase in wounded leaves. The systemic induction of LOX2, AOS, and vegetative storage protein was lower in the PLDalpha-suppressed plants than in wild-type plants, with AOS exhibiting a distinct pattern. These results indicate that activation of PLD mediates wound induction of JA and that LOX2 is probably a downstream target through which PLD promotes the production of JA.     

Phospholipase Dalpha3 is involved in the hyperosmotic response in Arabidopsis

Rapid activation of phospholipase D (PLD), which hydrolyzes membrane lipids to generate phosphatidic acid (PA), occurs under various hyperosmotic conditions, including salinity and water deficiency. The Arabidopsis thaliana PLD family has 12 members, and the function of PLD activation in hyperosmotic stress responses has remained elusive. Here, we show that knockout (KO) and overexpression (OE) of previously uncharacterized PLDalpha3 alter plant response to salinity and water deficit. PLDalpha3 uses multiple phospholipids as substrates with distinguishable preferences, and alterations of PLDalpha3 result in changes in PA level and membrane lipid composition. PLDalpha3-KO plants display increased sensitivities to salinity and water deficiency and also tend to induce abscisic acid-responsive genes more readily than wild-type plants, whereas PLDalpha3-OE plants have decreased sensitivities. In addition, PLDalpha3-KO plants flower later than wild-type plants in slightly dry conditions, whereas PLDalpha3-OE plants flower earlier. These data suggest that PLDalpha3 positively mediates plant responses to hyperosmotic stresses and that increased PLDalpha3 expression and associated lipid changes promote root growth, flowering, and stress avoidance.     

Regulation of plant water loss by manipulating the expression of phospholipase Dα

Phospholipase D (PLD) has been implicated in various processes, including signal transduction, membrane trafficking, and membrane degradation. Multiple forms of PLD with distinct biochemical properties have been described in the cell. In Arabidopsis, PLDalpha and PLDgamma, but not PLDbeta, were detected in guard cells, and antisense suppression resulted in a specific loss of PLDalpha. The abrogation of PLDalpha rendered plants less sensitive to abscisic acid and impaired stomatal closure induced by water deficits. PLDalpha-depleted plants exhibited accelerated transpirational water loss and a decreased ability to tolerate drought stress. Overexpression of PLDalpha enhanced the leaf's sensitivity to abscisic acid. These findings provide molecular and physiological evidence that PLDalpha plays a crucial role in regulating stomatal movement and plant-water status.     

Quantitative profiling of polar glycerolipid species from organs of wild-type Arabidopsis and a phospholipase Dalpha1 knockout mutant

Lipid profiling is a targeted metabolomics platform that provides a comprehensive analysis of lipid species with high sensitivity. Profiling based on electrospray ionization tandem mass spectrometry (ESI-MS/MS) provides quantitative data and is adaptable to high throughput analyses. Here we report the profiling of 140 apparent molecular species of polar glycerolipids in Arabidopsis leaves, flower stalks, flowers, siliques, roots, and seeds. Considerable differences in lipid species occur among these organs, providing insights into the different lipid metabolic activities in a specific organ. In addition, comparative profiling between wild-type and a knockout mutant pldalpha1 (locus ID: AT3G15730) provides insight into the metabolic function of phospholipase D (PLD) in different organs. PLDalpha1 contributes significantly to phosphatidic acid (PA) levels in roots, seeds, flowers, and flower stalks, but little to basal PA levels in siliques and leaves. In seeds of the pldalpha1 mutant plants, levels of PA, lysophosphatidylcholine, and lysophosphatidylethanolamine were significantly lower than those of wild-type seeds, suggesting a role for PLDalpha1 in membrane lipid degradation in seeds.