HEAT-SHOCK, DECILIATION AND RELEASE FROM ANOXIA INDUCE THE SYNTHESIS OF THE SAME SET OF POLYPEPTIDES IN STARVED T-PYRIFORMIS
HEAT-SHOCK, DECILIATION AND RELEASE FROM ANOXIA INDUCE THE SYNTHESIS OF THE SAME SET OF POLYPEPTIDES IN STARVED T-PYRIFORMIS
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DOI：
10.1016/0092-8674(80)90177-4
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发表时间：
1980-01-01
期刊：
影响因子：
64.5
通讯作者：
GOROVSKY, MA
中科院分区：
文献类型：
--
作者：
GUTTMAN, SD;GLOVER, CVC;GOROVSKY, MA
热休克、脱附和缺氧释放导致饥饿T.梨形。在每种情况下，合成相同的一组（至少）16个多肽的诱导，和许多这些多肽的积累在50分钟内的可接受的量。这些应激蛋白（SP）的MW，是非常相似的果蝇的热休克多肽。热休克和脱附导致与分离的细胞核相关的蛋白质发生类似的变化。一种应激诱导的多肽，命名为sp29c，在细胞核中高度富集。这种蛋白质在对照细胞中检测不到，但在应激反应中合成，并在50分钟内在细胞核中以100%的量积累。葡萄球菌核酸酶消化不会释放这种蛋白质，这表明它与染色质无关。其他应激诱导蛋白，sp 73和sp 75 a和B，也存在于从应激细胞分离的细胞核中，但与sp 29 c不同，在该隔室中不富集。另一种蛋白质在对照细胞的细胞质中大量存在，在应激后似乎移位到细胞核。
Heat shock, deciliation and release from anoxia result in similar alterations in the pattern of protein synthesis in starved T. pyriformis. In each case, synthesis of the same set of (at least) 16 polypeptides is induced, and many of these polypeptides accumulate in stainable amounts within 50 min. The MW of these stress proteins (sp), are very similar to those of the heat shock polypeptides of Drosophila. Heat shock and deciliation lead to similar changes in proteins associated with isolated nuclei. One stress-induced polypeptide, designated sp29c, is highly enriched in the nucleus. This protein is undetectable in control cells but is synthesized in response to stress and accumulates in the nucleus in stainable amounts within 50 min. It is not released by staphylococcal nuclease digestion, suggesting that it is not chromatin-associated. Other stress-induced proteins, sp73 and sp75a and b, also are present in nuclei isolated from stressed cells but, unlike sp29c, are not enriched in this compartment. Another protein, which is present in stainable quantities in the cytoplasm of control cells, appears to be translocated to the nucleus after stress.