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首页> 外文期刊>The Journal of Infectious Diseases >The Bacterial Stress-Responsive Hsp90 Chaperone (HtpG) Is Required for the Production of the Genotoxin Colibactin and the Siderophore Yersiniabactin in Escherichia coli
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The Bacterial Stress-Responsive Hsp90 Chaperone (HtpG) Is Required for the Production of the Genotoxin Colibactin and the Siderophore Yersiniabactin in Escherichia coli

机译：细菌应激反应的Hsp90伴侣（HtpG）是在大肠杆菌中生产基因毒素Colibactin和铁载体耶尔森菌素所必需的

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摘要

The genotoxin colibactin, synthesized by Escherichia coli, is a secondary metabolite belonging to the chemical family of hybrid polyketideonribosomal peptide compounds. It is produced by a complex biosynthetic assembly line encoded by the pks pathogenicity island. The presence of this large cluster of genes in the E. coli genome is invariably associated with the high-pathogenicity island, encoding the siderophore yersiniabactin, which belongs to the same chemical family as colibactin. The E. coli heat shock protein HtpG (Hsp90(Ec)) is the bacterial homolog of the eukaryotic molecular chaperone Hsp90, which is involved in the protection of cellular proteins against a variety of environmental stresses. In contrast to eukaryotic Hsp90, the functions and client proteins of Hsp90(Ec) are poorly known. Here, we demonstrated that production of colibactin and yersiniabactin is abolished in the absence of Hsp90(Ec). We further characterized an interplay between the Hsp90(Ec) molecular chaperone and the ClpQ protease involved in colibactin and yersiniabactin synthesis. Finally, we demonstrated that Hsp90(Ec) is required for the full in vivo virulence of extraintestinal pathogenic E. coli. This is the first report highlighting the role of heat shock protein Hps90(Ec) in the production of two secondary metabolites involved in E. coli virulence.
机译：大肠杆菌合成的基因毒素杆菌素是次生代谢产物，属于杂聚酮化合物/非核糖体肽化合物的化学家族。它是由pks致病岛编码的复杂生物合成装配线生产的。大肠杆菌基因组中这种大型基因簇的存在总是与高致病性岛相关联，该岛编码铁载体耶尔西菌素，与大肠菌素属于同一化学家族。大肠杆菌热休克蛋白HtpG（Hsp90（Ec））是真核分子伴侣Hsp90的细菌同源物，它参与保护细胞蛋白抵抗各种环境胁迫。与真核Hsp90相反，Hsp90（Ec）的功能和客户蛋白尚不清楚。在这里，我们证明了在没有Hsp90（Ec）的情况下，大肠菌素和耶尔西菌素的生产被废除了。我们进一步表征了Hsp90（Ec）分子伴侣和参与大肠杆菌素和耶尔西菌素合成的ClpQ蛋白酶之间的相互作用。最后，我们证明了Hsp90（Ec）是肠道外致病性大肠杆菌的完整体内毒力所必需的。这是第一个强调热休克蛋白Hps90（Ec）在涉及大肠杆菌毒力的两个次级代谢产物生产中的作用的报告。

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