Coca M A, Almoguera C, Jordano J
Instituto de Recursos Naturales y Agrobiología, C.S.I.C., Sevilla, Spain.
Plant Mol Biol. 1994 Jun;25(3):479-92. doi: 10.1007/BF00043876.
We isolated and sequenced Ha hsp17.9, a DNA complementary (cDNA) of dry-seed stored mRNA that encodes a low-molecular-weight heat-shock protein (LMW HSP). Sequence analysis identified Ha hsp17.9, and the previously reported Ha hsp17.6, as cDNAs encoding proteins (HSP17.6 and HSP17.9) which belong to different families of cytoplasmic LMW HSPs. Using specific antibodies we observed differential expression of both proteins during zygotic embryogenesis under controlled environment, and a remarkable persistence of these LMW HSPs during germination. Immuno-blot analysis of HSP17.9 proteins in two-dimensional gels revealed that the polypeptides expressed in embryos were indistinguishable from LMW HSPs expressed in vegetative tissues in response to water deficit; but they appeared different from homologous proteins expressed in response to thermal-stress. Tissue-print immunolocalization experiments showed that HSP17.9 and HSP17.6 were homogeneously distributed in every tissue of desiccation-tolerant dry seeds and young seedlings under non-stress conditions. These results demonstrate developmental regulation of specific, cytoplasmic, plant LMW HSPs, suggesting also their involvement in water-stress tolerance.
我们分离并测序了Ha hsp17.9,它是干燥种子储存mRNA的DNA互补(cDNA),编码一种低分子量热休克蛋白(LMW HSP)。序列分析确定Ha hsp17.9以及先前报道的Ha hsp17.6为编码蛋白质(HSP17.6和HSP17.9)的cDNA,这些蛋白质属于细胞质LMW HSP的不同家族。我们使用特异性抗体观察了在可控环境下合子胚发育过程中这两种蛋白质的差异表达,以及这些LMW HSP在萌发过程中的显著持续性。二维凝胶中HSP17.9蛋白质的免疫印迹分析表明,胚胎中表达的多肽与营养组织中响应水分亏缺而表达的LMW HSP无法区分;但它们与响应热胁迫而表达的同源蛋白质有所不同。组织印迹免疫定位实验表明,在非胁迫条件下,HSP17.9和HSP17.6在耐干燥干种子和幼苗的每个组织中均匀分布。这些结果证明了特定的细胞质植物LMW HSP的发育调控,也表明它们参与了水分胁迫耐受性。