APPPPA, HEAT-SHOCK STRESS, AND CELL OXIDATION
APPPPA, HEAT-SHOCK STRESS, AND CELL OXIDATION
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DOI：
10.1073/pnas.80.24.7496
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发表时间：
1983-01-01
期刊：
影响因子：
--
通讯作者：
AMES, BN
中科院分区：
文献类型：
--
作者：
LEE, PC;BOCHNER, BR;AMES, BN
鼠伤寒沙门氏菌LT 2诱导一组类似于先前在大肠杆菌中发现的热休克蛋白。这些蛋白质实际上是在温度从28 ℃转变后合成的唯一蛋白质。到50度。C.利用二维薄层色谱系统对腺苷酸进行分离，发现S。菌和大肠大肠杆菌积累P1，P4-二腺苷-5 ''-四磷酸（AppppA），P1-（腺苷-5“）-P3-（鸟苷-3”-二磷酸-5“）-三磷酸（ApppGpp）、P1-（腺苷-5”）-P4-（鸟苷-5“）-四磷酸（AppppG）、P1-（腺苷-5”）-P3-（鸟苷-5“）-三磷酸（ApppG）和P1，P3-二腺苷-5”-三磷酸（ApppA）。这些相同的腺苷酸化核苷酸在暴露于乙醇后积累，乙醇也是一种已知在多种细胞中诱导热休克反应的试剂。先前已证明在氧化强制降解条件下，AppppA、AppppGpp、AppppG、AppppG和AppppA会蓄积。这些腺苷酰化核苷酸可以是丙氨酸，即，调节分子，警告细胞氧化应激的开始。这些二核苷酸在热休克反应中积累的发现表明，氧化和热休克对细胞有共同的生理作用。这些二核苷酸可能是这些应激的信号，并触发热休克反应。
Salmonella typhimurium LT2 induces a set of heat-shock proteins analogous to those found previously in Escherichia coli. These are virtually the only proteins synthesized after a temperature shift from 28.degree. to 50.degree. C. Using a 2-dimensional TLC system developed to resolve adenylylated nucleotides, it was found that S. typhimurium and E. coli accumulate P1,P4-diadenosine-5''-tetraphosphate (AppppA), P1-(adenosine-5'')-P3-(guanosine-3''-diphosphate-5'')-triphosphate (ApppGpp), P1-(adenosine-5'')-P4-(guanosine-5'')-tetraphosphate (AppppG), P1-(adenosine-5'')-P3-(guanosine-5'')-triphosphate (ApppG), and P1,P3-diadenosine-5''-triphosphate (ApppA) after heat shock. These same adenylylated nucleotides accumulate after exposure to ethanol, an agent also known to induce the heat-shock response in a variety of cells. AppppA, ApppGpp, AppppG, ApppG and ApppA were previously shown to accumulate under conditions of oxidation stress. These adenylylated nucleotides may be alarmones, i.e., regulatory molecules, alerting cells to the onset of oxidation stress. The finding that these dinucleotides accumulate in response to heat shock suggests that oxidiation and heat shock have a common physiological effect on cells. These dinucleotides may signal the onset of these stresses and trigger the heat-shock response.