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1.
Pollen grains may become desiccated after independence from parent plants and remain viable in an inactive dry state during presentation and dispersal, until the conditions for rehydration and germination are prepared. But some pollen types do not tolerate the desiccation state and lose the germination power soon after release, and therefore, are difficult to store. In this study, moisture content, germinability, cytology and dehydrin and phenolics contents were surveyed in pistachio pollen at fresh and desiccated states. Mature pollen lost 54.1% of its initial moisture after 48 h desiccation along with severe decrease in germinability. Light microscopy results indicated that a low rate of pollen grains have vegetative cell rupture caused by desiccation, but a higher rate of grains were intact in appearance. Numerous amyloplasts persisted after desiccation as a sensitivity indicator. A 16 kDa dehydrin band was detected by western blot method with higher content in desiccated than fresh samples. High performance liquid chromatography (HPLC) analysis showed that the total content of phenolics increased slightly by desiccation. These results indicate the insufficiency of dehydrin and phenolics accumulation for achievement of desiccation tolerance. Furthermore, the severe loss of germinability in desiccated pistachio pollen may be the result of deficiency in some other protective mechanisms that need further investigations.  相似文献   
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Pea dehydrins: identification,characterisation and expression   总被引:3,自引:0,他引:3  
An antiserum raised against dehydrin from maize (Zea mays) recognised several polypeptides in extracts of pea (Pisum sativum) cotyledons. A cDNA expression library was prepared from mRNA of developing cotyledons, screened with the antiserum and positive clones were purified and characterised. The nucleotide sequence of one such clone, pPsB12, contained an open reading frame which would encode a polypeptide with regions of significant amino acid sequence similarity to dehydrins from other plant species.The deduced amino acid sequence of the pea dehydrin encoded by B12 is 197 amino acids in length, has a high glycine content (25.9%), lacks tryptophan and is highly hydrophilic. The polypeptide has an estimated molecular mass of 20.4 kDa and pI=6.4. An in vitro synthesised product from the clone comigrates with one of the in vivo proteins recognised by the antiserum.A comparison of the pea dehydrin sequence with sequences from other species revealed conserved amino acid regions: an N-terminal DEYGNP and a lysine-rich block (KIKEKLPG), both of which are present in two copies. Unexpectedly, pea dehydrin lacks a stretch of serine residues which is conserved in other dehydrins.B12 mRNA and dehydrin proteins accumulated in dehydration-stressed seedlings, associated with elevated levels of endogenous abscisic acid (ABA). Applied ABA induced expression of dehydrins in unstressed seedlings. Dehydrin expression was rapidly reversed when seedlings were removed from the stress or from treatment with ABA and placed in water.During pea cotyledon development, dehydrin mRNA and proteins accumulated in mid to late embryogenesis. Dehydrin proteins were some of the most actively synthesised at about the time of maximum fresh weight and represent about 2% of protein in mature cotyledons.  相似文献   
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小麦类脱水素的表达、纯化及多克隆抗体的制备   总被引:1,自引:0,他引:1  
脱水素在胚胎发育后期累积,外源脱落酸(ABA)、低温、干旱和其他一些环境条件下能诱导脱水素的产生,尽管植物在脱水条件下脱水素广泛存在于细胞中,但其生化功能仍不清楚.为研究小麦在不同时期脱水素基因的表达情况和生物学功能及抗体制备,以小麦幼芽为材料,经干旱胁迫处理后,提取总RNA,通过RT-PCR得到小麦类脱水素基因片段(WZY1-1),再连接至克隆载体PUCM-T,并成功构建重组表达质粒PET-32a( )-wzy1-1,将阳性重组质粒转化于受体菌BL21(DE3)感受态细胞中,经IPTG诱导表达,进行表达产物的聚丙烯酰胺凝胶电泳(SDS-PAGE)检测.结果表明,表达蛋白位于37ku处,小麦类脱水素基因获得高效表达.表达蛋白经Ni2 琼脂糖凝胶亲和层析和透析袋电洗脱法纯化后,对兔子进行免疫,制备的抗血清通过ELISA检测到较高的多克隆抗体效价.蛋白质印迹结果显示,利用纯化的蛋白质制备的兔抗血清可以很好地和所表达的蛋白质带特异性结合,且郑引1号小麦幼苗进行干旱处理,提取粗蛋白,SDS-PAGE,蛋白质印迹检测显示,在分子质量28ku处出现特异的蛋白质条带,这说明所制备的抗血清可以与小麦叶片所表达的dehydrin蛋白特异性结合,证明其具有良好的免疫原性.  相似文献   
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Dehydrins are a family of proteins that accumulate in response to abiotic stresses. Little is known about the biochemical functions of these proteins. It is known that the Arabidopsis dehydrin, ERD14, is activated by phosphorylation to bind calcium and other ions. To begin to categorize the Arabidopsis dehydrins into functional families, we determined whether representative members of the dehydrin sub families share the properties of ERD14. When phosphorylated in vitro with casein kinase II; recombinant COR47, and ERD10 (and ERD14) become activated to bind calcium. ERD14 exhibited the highest calcium-binding activity followed by ERD10 and COR47. These dehydrins, when isolated from cold-treated Arabidopsis plants were also shown to have phosphorylation-dependent, calcium-binding activity. RAB18 showed very little calcium binding activity, even though it was phosphorylated by casein kinase II. XERO2 was not phosphorylated with CKII and did not bind calcium. Competition studies suggest that other divalent cations may bind to the dehydrins COR47, ERD10, and ERD14. Utilizing matrix-assisted laser desorption ionization – time of flight mass spectroscopy (MALDI-TOF), we determined that the poly serine region located in all three calcium-binding family members (COR47, ERD10, and ERD14) is the most likely phosphorylation site responsible for the activation of calcium binding. These results are consistent with a distinct biochemical function for the acidic subclass of dehydrins (COR47, ERD10, and ERD14) as ion (calcium)-interacting proteins.  相似文献   
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Stress-induced accumulation of five (COR47, LTI29, ERD14, LTI30 and RAB18) and tissue localization of four (LTI29, ERD14, LTI30 and RAB18) dehydrins in Arabidopsis were characterized immunologically with protein-specific antibodies. The five dehydrins exhibited clear differences in their accumulation patterns in response to low temperature, ABA and salinity. ERD14 accumulated in unstressed plants, although the protein level was up-regulated by ABA, salinity and low temperature. LTI29 mainly accumulated in response to low temperature, but was also found in ABA- and salt-treated plants. LTI30 and COR47 accumulated primarily in response to low temperature, whereas RAB18 was only found in ABA-treated plants and was the only dehydrin in this study that accumulated in dry seeds.Immunohistochemical localization of LTI29, ERD14 and RAB18 demonstrated tissue and cell type specificity in unstressed plants. ERD14 was present in the vascular tissue and bordering parenchymal cells, LTI29 and ERD14 accumulated in the root tip, and RAB18 was localized to stomatal guard cells. LTI30 was not detected in unstressed plants. The localization of LTI29, ERD14 and RAB18 in stress-treated plants was not restricted to certain tissues or cell types. Instead these proteins accumulated in most cells, although cells within and surrounding the vascular tissue showed more intense staining. LTI30 accumulated primarily in vascular tissue and anthers of cold-treated plants.This study supports a physiological function for dehydrins in certain plant cells during optimal growth conditions and in most cell types during ABA or cold treatment. The differences in stress specificity and spatial distribution of dehydrins in Arabidopsis suggest a functional specialization for the members of this protein family.  相似文献   
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刘兰  张林生  邢媛  张楠 《西北植物学报》2011,31(9):1786-1792
以2种耐旱性不同的盆栽小麦陕合6号(干旱耐受型)和郑引1号(干旱敏感型)为材料,分别在其苗期、分蘖期、拔节期、开花期对土壤实施不同程度的自然干旱胁迫和复水处理,采用SDS-PAGE和Western blotting技术研究其叶片脱水素的表达规律,探究小麦整个生长期脱水素的表达与干旱胁迫的关系.结果表明:2种小麦的脱水素均仅在干旱胁迫时表达,其中45 kD和37 kD的脱水素在2种小麦的4个发育期的叶片中均有表达,28 kD的脱水素仅在特定发育时期表达.在干旱耐受型小麦(陕合6号)中,脱水素在胁迫初期少量表达,随着胁迫程度加剧表达量急剧增加,在重度干旱胁迫下达到峰值,复水后小麦叶片中脱水素含量迅速下降;在干旱敏感型小麦(郑引1号)中,脱水素在胁迫初期大量表达,中度胁迫表达量小幅度回落,到复水1 d达到峰值,此后随着复水时间增加小麦叶片中脱水素的量逐渐下降.研究表明,小麦叶片脱水素表达与干旱胁迫程度和生育期迫密切相关,不同耐旱型小麦材料中叶片脱水素表达的差异与品种之间的干旱耐受能力密切相关.  相似文献   
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