Department of Plant Biology, University of Illinois, Urbana, Illinois 61801.
Plant Physiol. 1984 Jun;75(2):431-41. doi: 10.1104/pp.75.2.431.
The tissue specificity of the heat-shock response in maize was investigated. The ability to synthesize heat shock proteins (hsp) at 40 degrees C, as well as the intensity and duration of that synthesis, was analyzed in coleoptiles, scutella, green and etiolated leaves, suspension-cultured cells, germinating pollen grains, and primary root sections at different stages of development. One-dimensional sodium dodecyl sulfate gel electrophoresis of extracted proteins revealed that most of the tissues synthesized the typical set of 10 hsp, but that the exact characteristics of the response depended upon the tissue type. While elongating portions of the primary root exhibited a strong heat shock response, the more mature portions showed a reduced ability to synthesize hsp. Leaves, whether green or etiolated, excised or intact, constitutively synthesized a low level of hsp at 25 degrees C, and high levels could be induced at 40 degrees C. Suspension-cultures of Black Mexican sweet corn synthesized, besides the typical set of hsp, two additional polypeptides. In contrast to all the other tissues, germinating pollen grains could not be induced to synthesize the typical set of hsp but did synthesize two new polypeptides of 92 and 56 kD molecular weight.The heat shock response was transient for most of the tissues which synthesized the standard set of hsp. Hsp synthesis was detected up to 2 to 3 hours, but not at 10 hours of continuous 40 degrees C treatment. The exception was suspension cultured cells, in which hsp synthesis showed only a slight reduction after 10 hours at 40 degrees C. Tissue-specific differences in the heat-shock response suggest that there are differences in the way a given tissue is able to adapt to high temperature.We have confirmed the previous suggestion that maize hsp do not accumulate in substantial quantities. Using two-dimensional gel analysis, hsp could be detected by autoradiography but not by sensitive silver staining techniques.
我们研究了玉米热激反应的组织特异性。在 40℃下合成热休克蛋白(hsp)的能力,以及该合成的强度和持续时间,在胚芽鞘、盾片、绿色和黄化叶片、悬浮培养细胞、萌发花粉粒和不同发育阶段的主根切片中进行了分析。提取蛋白的一维十二烷基硫酸钠凝胶电泳显示,大多数组织合成了典型的 10 种 hsp,但反应的确切特征取决于组织类型。尽管主根的伸长部分表现出强烈的热激反应,但更成熟的部分合成 hsp 的能力降低。无论是绿色还是黄化、离体还是完整的叶片,在 25℃下均持续合成低水平的 hsp,在 40℃下可诱导高水平的 hsp。黑墨西哥甜玉米的悬浮培养物除了合成典型的 hsp 外,还合成了两种额外的多肽。与所有其他组织相反,萌发花粉粒不能诱导合成典型的 hsp,但可以合成两种新的 92 和 56 kD 分子量的多肽。大多数合成标准 hsp 的组织的热激反应是短暂的。hsp 的合成可检测到长达 2 到 3 小时,但在连续 40℃处理 10 小时时则无法检测到。悬浮培养细胞是个例外,在 40℃下培养 10 小时后 hsp 合成仅略有减少。组织特异性的热激反应差异表明,组织适应高温的方式存在差异。我们证实了以前的建议,即玉米 hsp 不会大量积累。使用二维凝胶分析,hsp 可以通过放射自显影检测到,但不能通过敏感的银染技术检测到。