Peptidoglycan hydrolysis is required for assembly and activity of the transenvelope secretion complex during sporulation in Bacillus subtilis.

Peptidoglycan hydrolysis is required for assembly and activity of the transenvelope secretion complex during sporulation in Bacillus subtilis.
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DOI:
10.1111/mmi.12322
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发表时间:
2013-09
影响因子:
3.6
通讯作者:
Rudner DZ
Rudner DZ
中科院分区:
生物学2区
文献类型:
--
作者:
Rodrigues CD;Marquis KA;Meisner J;Rudner DZ

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产孢子的枯草芽孢杆菌细胞组装一个跨膜分泌物复合体,连接母细胞和发育中的孢子。前孔蛋白SpoIIQ和母细胞蛋白SpoIIIAH通过双膜隔膜相互作用,并被认为组装成一个通道,作为这一专门分泌系统的基底层。SpoIIQ绝对需要将SpoIIIAH招募到母细胞侧的孢子形成隔膜上,然而SpoIIQ定位的机制尚不清楚。在这里,我们证明了SpoIIQ的定位需要它的伴侣蛋白SpoIIIAH和两个细胞壁水解酶SpoIID和SpoIIP降解隔膜肽聚糖(PG)。我们的数据表明,PG的降解使第二个母细胞产生的蛋白质能够与SpoIIQ相互作用。两种母细胞锚定机制都被禁用的细胞存在协同产孢子缺陷,这表明两种定位因子都在分泌复合体中发挥作用。最后,我们证明隔膜PG的降解对于活性复合体的组装是至关重要的。总之,这些结果表明,连接母细胞和前孔的专门分泌系统具有接近革兰氏阴性细菌的复杂性,并揭示了产孢细胞必须克服类似的挑战,才能组装跨包膜复合体。
Sporulating Bacillus subtilis cells assemble a transenvelope secretion complex that connects the mother cell and developing spore. The forespore protein SpoIIQ and the mother-cell protein SpoIIIAH interact across the double membrane septum and are thought to assemble into a channel that serves as the basement layer of this specialized secretion system. SpoIIQ is absolutely required to recruit SpoIIIAH to the sporulation septum on the mother-cell side, however the mechanism by which SpoIIQ is localized has been unclear. Here, we show that SpoIIQ localization requires its partner protein SpoIIIAH and degradation of the septal peptidoglycan (PG) by the two cell wall hydrolases SpoIID and SpoIIP. Our data suggest that PG degradation enables a second mother-cell-produced protein to interact with SpoIIQ. Cells in which both mother-cell anchoring mechanisms have been disabled have a synergistic sporulation defect suggesting that both localization factors function in the secretion complex. Finally, we show that septal PG degradation is critical for the assembly of an active complex. Altogether, these results suggest that the specialized secretion system that links the mother cell and forespore has a complexity approaching those found in Gram-negative bacteria and reveal that the sporulating cell must overcome similar challenges in assembling a transenvelope complex.
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