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首页> 外文期刊>Genes to cells : >Characterization of HscC (Hsc62), homologue of Hsp70 in Escherichia coli: over-expression of HscC modulates the activity of house keeping sigma factor sigma70.
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Characterization of HscC (Hsc62), homologue of Hsp70 in Escherichia coli: over-expression of HscC modulates the activity of house keeping sigma factor sigma70.

机译：HscC（Hsc62）的特性，是大肠杆菌中Hsp70的同源物：HscC的过表达调节了家政西格玛因子sigma70的活性。

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BACKGROUND: HscC, the third member of the Hsp70 family in Escherichia coli, shares 33% identity with the other two homologues, DnaK and HscA, and displays ATPase activity. Genetic and biochemical evidence indicates that the DnaK-DnaJ chaperone system interacts with sigma32 and is involved in the negative regulation of the heat shock response. Although HscC is a highly conserved protein in the Hsp70 family, its function is still unknown. RESULTS: We observed that the over-expression of HscC caused severe growth inhibition. To explore this effect, we performed primer extension analysis and a beta-galactosidase assay and found that HscC reduced the sigma70-dependent promoter activity. An in vitro transcription assay revealed that HscC inhibited sigma70-dependent transcription. In addition, the co-purification analysis showed that sigma70 co-eluted with HscC. CONCLUSION: These results indicate that HscC forms a complex with sigma70 and may function as its negative modulator.
机译：背景：HscC是大肠杆菌Hsp70家族的第三个成员，与其他两个同系物DnaK和HscA具有33％的同一性，并显示ATPase活性。遗传和生化证据表明，DnaK-DnaJ分子伴侣系统与sigma32相互作用，并参与了热激反应的负调控。尽管HscC在Hsp70家族中是高度保守的蛋白质，但其功能仍然未知。结果：我们观察到HscC的过表达引起严重的生长抑制。为了探索这种效果，我们进行了引物延伸分析和β-半乳糖苷酶测定，发现HscC降低了sigma70依赖性启动子活性。体外转录试验显示，HscC抑制sigma70依赖性转录。此外，共纯化分析表明sigma70与HscC共洗脱。结论：这些结果表明，HscC与sigma70形成复合物，并可能充当其负调控因子。

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