HEAT-SHOCK PROTEINS ARE METHYLATED IN AVIAN AND MAMMALIAN-CELLS
HEAT-SHOCK PROTEINS ARE METHYLATED IN AVIAN AND MAMMALIAN-CELLS
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DOI：
10.1073/pnas.78.6.3531
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发表时间：
1981-01-01
期刊：
影响因子：
--
通讯作者：
LAZARIDES, E
中科院分区：
文献类型：
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作者：
WANG, C;GOMER, RH;LAZARIDES, E
将在组织培养中生长的鸡细胞暴露于热休克或亚砷酸钠导致3种主要多肽的合成急剧增加，其分子量为83，000（HSP 83）、68，000（HSP 68;热蛋白）和25，000（HSP 25）。在相同条件下孵育BHK-21（幼仓鼠肾）或HeLa（人宫颈癌）细胞导致HSP 68和66，000-道尔顿多肽（HSP 66）的诱导。鸡热蛋白等电聚焦分解成一个主要的酸性和碱性成分;哺乳动物热蛋白只分解成一个主要的酸性成分。HSP 83和酸性形式的热蛋白是高度保守的，在所有的鸟类和哺乳动物细胞检查，判断其电泳迁移率，等电点和1维肽图。热蛋白的酸性形式与与脑微管共纯化的蛋白质是不可区分的，并且与在组织培养中生长的细胞的中间体富集的Triton/KCl细胞骨架保持相关。Thermin也是骨骼肌原纤维的组分。HSP 83和热蛋白在正常生长条件下培养的细胞中被甲基化。在亚砷酸钠存在下孵育细胞诱导热休克蛋白，导致新合成的热蛋白显著甲基化。在相同的实验条件下，没有观察到HSP 83甲基化的显著增加。HSP 25在未处理的细胞或用亚砷酸钠处理的细胞中不甲基化。热休克蛋白的甲基化可能在调节其功能中起重要作用。
Exposure of chicken cells grown in tissue culture to heat shock or sodium arsenite results in a dramatic increase in the synthesis of 3 major polypeptides with MW of 83,000 (HSP 83), 68,000 (HSP 68; thermin), and 25,000 (HSP 25). Incubation of BHK-21 (baby hamster kidney) or HeLa (human cervical carcinoma) cells under the same conditions results in induction of HSP 68 and a 66,000-dalton polypeptide (HSP 66). Chicken thermin is resolved by isoelectric focusing into a major acidic and a more-basic component; mammalian thermin is resolved only into 1 major acidic component. HSP 83 and the acidic form of thermin are highly conserved in all avian and mammalian cells examined as judged by their electrophoretic mobilities, isoelectric points and 1-dimensional peptide maps. The acidic form of thermin is indistinguishable from a protein that copurifies with brain microtubules and that remains associated with the intermediate filament-enriched Triton/KCl cytoskeletons of cells grown in tissue culture. Thermin is also a component of skeletal myofibrils. HSP 83 and thermin are methylated in cells cultured under normal growth conditions. Induction of heat shock proteins by incubation of cells in the presence of sodium arsenite results in a marked methylation of the newly synthesized thermin. Under the same experimental conditions, no significant increase in methylation of the HSP 83 is observed. HSP 25 is not methylated in untreated cells or in cells treated with sodium arsenite. Methylation of heat shock proteins may have an important role in regulating their function.