Characterisation of chloroplast heat shock proteins in young leaves of C4 monocotyledons
Characterisation of chloroplast heat shock proteins in young leaves of C4 monocotyledons
复制标题
C4单子叶植物幼叶叶绿体热激蛋白的表征
DOI：
10.1111/j.1399-3054.1994.tb06663.x
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发表时间：
1994
影响因子：
6.4
通讯作者：
C. Critchley
中科院分区：
文献类型：
--
作者：
A. Clarke;C. Critchley
高粱叶绿体蛋白的体内放射性标记。CV. Texas 610）叶片中的热休克蛋白（HSP），并通过一维电泳对其进行分离，揭示了至少6种24至94 kDa之间的热休克蛋白（HSP）。其中24 kDa蛋白质是最突出的。所有这些叶绿体热休克蛋白被发现只在基质中。在使用二维电泳进行更仔细的检查后，证明24 kDa热休克蛋白是两种大小相似的热休克多肽，具有相同的分子量和radiohel掺入水平，但等电点略有不同，表明是异构体。分离了另外两种单子叶植物（Punicum miliaceum L.）和伞形科（Umbilia panictrides L.）发现了相似的异构体每一个都是24 kDa。在所有三个物种中也观察到其他几个先前未鉴定的22和38 kDa之间的热休克蛋白。在粟粒草中。HSP中最突出的是一对24 kDa蛋白，而在U.黍类。35 ~ 38 kDa的HSP含量最高。在体内叶绿素荧光测量表明，没有持续的损害光合效率发生后，每个物种的热应力制度。然而，当细胞质蛋白质合成在高温处理过程中受到抑制，光合效率显着下降，表明叶绿体热休克蛋白可能具有保护作用。研究还表明，在这两种5的基质中均观察到约380 kDa的单个叶绿体HSP复合物。bicolor和P. miliaceum叶片。这是在对比较小的HSP复合物（200-265 kDa）在以前的研究中观察到的叶绿体热休克蛋白在C物种。
In vivo radiolabeling of chloroplast proteins in grain sorghum (Sorghum bicolor L. cv. Texas 610) leaves and their separation by one‐dimensional electrophoresis revealed at least 6 heat shock proteins (HSPs) between 24 and 94 kDa. of which the 24 kDa protein was the most prominent. All of these chloroplast heat shock proteins were found exclusively in the stroma. The 24 kDa heat shock protein, upon closer examination using two‐dimensional electrophoresis proved to be two similarly‐sized heat shock polypeptides with identical molecular masses and level of radiolahel incorporation, hut slightly different in isoeiectric points, suggesting isomers. Separation of stromal heat shock proteins synthesised in two other C monocotyledons (Punicum miliaceum L. and Umchloa panictrides L.) revealed similar putative isomers. each of 24 kDa. Several other, previously unidentified, heat shock proteins between 22 and 38 kDa were also observed in all three species. In P. miliaceum. the most prominent HSP was the pair of 24 kDa proteins, whereas in U. panicoides. it was a group of 35 to 38 kDa HSPs that was most abundant. In vivo chlorophyll fluorescence measurements showed that no sustained impairment to photosynthetic efficiency had occurred for each species after the heat stress regime. However, when cytoplasmic protein synthesis was inhibited during the high temperature treatment, a dramatic decrease was observed in photosynthetic efficiency, suggesting a possible protective role for chloroplast heat shock proteins. It was also shown that a single chloroplast HSP complex of around 380 kDa was observed in the stroma of both 5. bicolor and P. miliaceum leaves in vivo. This was in contrast to the smaller HSP complex (200–265 kDa) observed in previous studies on chloroplast heat shock proteins in C species.