...
首页> 外文期刊>Journal of bacteriology >Synthesis and degradation of nitrate reductase in Escherichia coli.
【24h】

Synthesis and degradation of nitrate reductase in Escherichia coli.

机译:大肠杆菌中硝酸盐还原酶的合成和降解。

获取原文
           

摘要

The biosynthesis, insertion, and in vivo stability of nitrate reductase were examined by following the amount of labeled enzyme present in both membranes and cytoplasm at varying times after a short pulse of radioactive sulfate. Nitrate reductase levels were measured by autoradiography of immunoprecipitated material after fractionation on sodium dodecyl sulfate-polyacrylamide gels. These experiments demonstrated that subunits A and B were synthesized in the cytoplasm and subsequently inserted into membranes. The insertion of these subunits was dependent upon the synthesis of another protein, and the rate of synthesis of this protein determined the rate of insertion of subunits A and B. The nitrate reductase produced by the chlA mutant was inserted into membranes in the normal fashion, whereas the nitrate reductase produced by the chlC and chlE mutants was poorly incorporated. The nitrate reductase in the wild type was completely stable in vivo under inducing or noninducing conditions, whereas in the chlC and chlE mutants nitrate reductase was degraded extensively in both the cytoplasm and membranes, even under inducing conditions. Under similar conditions, nitrate reductase was stable in the chlA mutant.
机译:通过追踪短时间放射性硫酸盐在不同时间存在于膜和细胞质中的标记酶的量来检查硝酸还原酶的生物合成,插入和体内稳定性。在十二烷基硫酸钠-聚丙烯酰胺凝胶上分级分离后,通过放射免疫沉淀材料的放射自显影测量硝酸还原酶的水平。这些实验证明亚基A和B在细胞质中合成,随后插入膜中。这些亚基的插入取决于另一种蛋白质的合成,该蛋白质的合成速率决定了亚基A和B的插入速率。chlA突变体产生的硝酸盐还原酶以正常方式插入膜中,而由chlC和chlE突变体产生的硝酸盐还原酶掺入很少。在诱导或非诱导条件下,野生型的硝酸还原酶在体内是完全稳定的,而在chlC和chlE突变体中,即使在诱导条件下,硝酸还原酶在细胞质和细胞膜中也被广泛降解。在相似的条件下,硝酸还原酶在chlA突变体中稳定。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号