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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The nonredundant roles of two 4′-phosphopantetheinyl transferases in vital processes of Mycobacteria
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The nonredundant roles of two 4′-phosphopantetheinyl transferases in vital processes of Mycobacteria

机译：在分枝杆菌的关键过程中两个4'-磷酸泛肽亚基转移酶的非冗余作用

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摘要

Mycobacterium tuberculosis contains > 20 enzymes that require activation by transfer of the 4′-phosphopantetheine moiety of CoA onto a conserved serine residue, a posttranslational modification catalyzed by 4′-phosphopantetheinyl transferases (PPTases). The modified proteins are involved in key metabolic processes such as cell envelope biogenesis and the production of virulence factors. We show that two PPTases conserved in all Mycobacterium spp. and in related genera activate two different subsets of proteins and are not functionally redundant. One enzyme, AcpS, activates the two fatty acid synthase systems of mycobacteria, whereas the other PPTase, PptT, acts on type-Ⅰ polyketide synthases and non-ribosomal peptide synthases, both of which are involved in the biosynthesis of virulence factors. We demonstrate that both PPTases are essential for Mycobacterium smegmatis viability and that PptT is required for the survival of Mycobacterium bovis bacillus Calmette-Guerin. These enzymes are thus central to the biology of mycobacteria and for mycobacterial pathogenesis and represent promising targets for new antituberculosis drugs.
机译：结核分枝杆菌含有> 20种酶，这些酶需要通过将CoA的4'-磷酸泛肽碱部分转移到保守的丝氨酸残基上来激活，该酶是4'-磷酸泛酰维生素A转移酶（PPTase）催化的翻译后修饰。修饰的蛋白质参与关键的代谢过程，例如细胞包膜的生物发生和毒力因子的产生。我们显示在所有分枝杆菌属物种中保守的两个PPTases。并且在相关属中激活两个不同的蛋白质子集，并且在功能上不是多余的。一种酶AcpS激活分枝杆菌的两个脂肪酸合酶系统，而另一种PPTase PptT作用于Ⅰ型聚酮合酶和非核糖体肽合酶，这两个酶均参与毒力因子的生物合成。我们证明这两种PPTases对于耻垢分枝杆菌的生存力都是必不可少的，并且PptT是牛分枝杆菌Calmette-Guerin生存的必需条件。因此，这些酶对于分枝杆菌的生物学和分枝杆菌的发病机理至关重要，并且代表了新的抗结核药物的有希望的靶标。

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