Expression of a 66-kD heat shock protein associated with the process of cyst formation of a true slime mold, Physarum polycephalum.
Expression of a 66-kD heat shock protein associated with the process of cyst formation of a true slime mold, Physarum polycephalum.
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与真正的粘菌多头绒泡菌的包囊形成过程相关的 66 kD 热休克蛋白的表达。
DOI：
10.1247/csf.17.301
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发表时间：
1992
影响因子：
1.5
通讯作者：
K. Murakami‐Murofushi
中科院分区：
文献类型：
--
作者：
Y. Shimada;T. Kasakura;M. Yokota;Y. Miyata;H. Murofushi;H. Sakai;I. Yahara;K. Murakami‐Murofushi
在不利的生长条件下，多头绒泡菌（Physarumpolycephalum）的单倍体黏变形虫收缩伪足，将细胞形状变为盘状，然后构建细胞壁形成微囊。单倍体细胞的这些形态变化与肌动蛋白丝细胞内分布的变化有关。鬼笔环肽染色显示，肌动蛋白丝几乎均匀地分布在整个细胞质的粘液阿米巴。当这些细胞转移到包囊诱导培养基中时，肌动蛋白结构变为短杆或点，之后杆/点在微包囊中消失。在囊肿诱导培养基中孵育的粘阿米巴引起的几种蛋白质的合成，其中66 kD的蛋白质是最显着的诱导。形态学变化和66-kD蛋白的诱导在升高的温度例如40 ℃下是显著的。然而，当同一物种的疟原虫在40 ℃下孵育时，66-kD蛋白没有被诱导。我们发现，66-kD蛋白与聚合肌动蛋白共沉淀，并结合到ATP-琼脂糖。用抗66-kD蛋白抗体和鬼笔环肽对盘状细胞进行双重染色，揭示了66-kD蛋白和肌动蛋白丝在短杆或点中的重叠定位。虽然66 kD蛋白的诱导在高温下增强，但该蛋白与常见的热休克蛋白HSP 70和HSP 90在免疫学上无关，这些蛋白在进化过程中高度保守。这些结果表明，66-kD蛋白是一种新的热休克蛋白，其特异性表达于包囊形成过程中。
Under unfavorable conditions for growth, haploid myxoamoebae of Physarum polycephalum retracted their pseudopodia and changed their cell shape into disk-like form, after which they constructed the cell walls to form microcysts. These morphological changes of haploid cells were associated with changes in intracellular distribution of actin filaments. Staining with phalloidin showed that actin filaments were almost uniformly distributed throughout the cytoplasm of the myxoamoebae. When these cells were transferred to a cyst-inducing medium, the actin structures changed into short rods or dots, after which the rods/dots disappeared in the microcysts. An incubation of the myxoamoebae in the cyst-inducing medium caused the synthesis of several proteins, among which a 66-kD protein was most prominently induced. The morphological changes and the induction of the 66-kD protein was pronounced at elevated temperatures, e.g. 40 degrees C. The 66-kD protein was not induced, however, when plasmodia of the same species were incubated at 40 degrees C. We found that the 66-kD protein was co-precipitated with polymerized actin and bound to ATP-agarose. A double staining of the disk-shaped cells with anti-66-kD protein antibody and phalloidin revealed superimposable localization of the 66-kD protein and actin filaments in the short rods or dots. Although the induction of the 66-kD protein was enhanced at high temperatures, the protein was immunologically unrelated to the common heat shock proteins, HSP70 and HSP90, those are highly conserved during evolution. These results indicate that the 66-kD protein is a novel heat shock protein which is specifically expressed during cyst formation.
体外高温下热休克蛋白 (Mr 70,000) 对蛋白质和 DNA 合成的影响。
影响因子：
11.2
作者：
Mivechi,NF;Ogilvie,PD
通讯作者：
Ogilvie,PD
90 kDa 热休克蛋白 (hsp-90) 具有 ATP 结合位点和自磷酸化活性。
DOI：
--
发表时间：
1991
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Csermely,P;Kahn,CR
通讯作者：
Kahn,CR