A GENE REGULATING THE HEAT-SHOCK RESPONSE IN ESCHERICHIA-COLI ALSO AFFECTS PROTEOLYSIS

A GENE REGULATING THE HEAT-SHOCK RESPONSE IN ESCHERICHIA-COLI ALSO AFFECTS PROTEOLYSIS
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DOI:
10.1073/pnas.81.21.6779
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发表时间:
1984-01-01
期刊:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子:
--
通讯作者:
GROSS, CA
GROSS, CA
中科院分区:
其他
文献类型:
--
作者:
BAKER, TA;GROSSMAN, AD;GROSS, CA

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大肠杆菌中的 htpR 位点编码热休克反应的调节因子。含有htpR165突变的细胞在高温下诱导热休克蛋白的合成方面存在缺陷。这些细胞在降解 2 种通常在 htpR+ 细胞中不稳定的蛋白质方面也存在缺陷。蛋白水解缺陷在 30°C 和 30°C 时都很明显。 C 和 42 度。 C. 使用标记救援技术将该缺陷定位到 htpR 基因座。尽管两种蛋白水解底物在lon-菌株中部分稳定,但htpR165菌株表现出的蛋白水解缺陷并不模拟lon-状态。 htpR165菌株在30℃下以正常速率合成Lon。 C并且不显示与长株相关的粘液性和辐射敏感性的表型。
The htpR locus in E. coli encodes a regulator on the heat shock response. Cells containing the htpR165 mutation are defective in the induction of synthesis of heat-shock proteins at high temperature. These cells are also defective in degrading 2 proteins that are normally unstable in htpR+ cells. The proteolytic defect is manifest at both 30.degree. C and 42.degree. C. A marker rescue technique was used to map this defect to the htpR locus. Although both proteolytic substrates are partially stabilized in lon- strains, the defect in proteolysis exhibited by the htpR165 strain does not mimic the lon- state. The htpR165 strain synthesizes Lon at the normal rate at 30.degree. C and does not show the phenotypes of mucoidy and radiation sensitivity associated with lon- strains.