Intrinsically disordered protein regions are required for cell wall homeostasis in Bacillus subtilis.
Intrinsically disordered protein regions are required for cell wall homeostasis in Bacillus subtilis.
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DOI：
10.1101/gad.349895.122
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发表时间：
2022-09-01
影响因子：
10.5
通讯作者：
Rudner, David Z. Z.
中科院分区：
文献类型：
--
作者：
Brunet, Yannick R. R.;Habib, Cameron;Brogan, Anna P. P.;Artzi, Lior;Rudner, David Z. Z.
关键词：
在这项研究中，Brunet等人研究了细菌中内在无序蛋白质区域（IDR）的作用，并报告枯草芽孢杆菌中的胞质外IDR是细胞壁稳态所需的。他们的数据支持这样一种模型，即抗σ因子RsgI上的IDR感知PG网络中的缺口并激活σI，而PBP 1上的IDR将合酶引导到这些位点以强化它们。内含子无序蛋白区（IDR）在真核生物中参与了多种细胞核和细胞质功能，但它们在细菌中的作用尚不清楚。在这里，我们报告说，在枯草芽孢杆菌胞质外的IDRs细胞壁的稳态。B。枯草杆菌σI转录因子通过其膜锚定抗σ因子RsgI的调节性膜内蛋白水解（RIP）响应于包膜应激而被激活。与典型的RIP途径，我们表明，胞外域（网站-1）裂解的RsgI是组成性的，但两个裂解产物保持稳定关联，防止膜内（网站-2）蛋白水解。该途径中的调节步骤是它们的解离，其由受损的细胞壁合成触发，并且需要RsgI的胞质外IDR。有趣的是，主要的肽聚糖聚合酶PBP 1也包含一个胞质外IDR，我们表明，这个区域是重要的，它的功能。不同的IDR可以取代RsgI和PBP 1上的本地IDR，认为这些非结构化区域的功能相似。我们的数据支持一个模型，其中RsgI-σI信号系统和PBP 1代表互补的途径来修复PG网络中的缺口。RsgI上的IDR感知这些缺口并激活σI，而PBP 1上的IDR将合酶引导至这些位点以强化它们。
In this study, Brunet et al. investigated the roles of intrinsically disordered protein regions (IDRs) in bacteria, and report that extracytoplasmic IDRs in Bacillus subtilis are required for cell wall homeostasis. Their data support a model in which the IDR on anti-σ factor RsgI senses gaps in the PG meshwork and activates σI, while the IDR on PBP1 directs the synthase to these sites to fortify them. Intrinsically disordered protein regions (IDRs) have been implicated in diverse nuclear and cytoplasmic functions in eukaryotes, but their roles in bacteria are less clear. Here, we report that extracytoplasmic IDRs in Bacillus subtilis are required for cell wall homeostasis. The B. subtilis σI transcription factor is activated in response to envelope stress through regulated intramembrane proteolysis (RIP) of its membrane-anchored anti-σ factor, RsgI. Unlike canonical RIP pathways, we show that ectodomain (site-1) cleavage of RsgI is constitutive, but the two cleavage products remain stably associated, preventing intramembrane (site-2) proteolysis. The regulated step in this pathway is their dissociation, which is triggered by impaired cell wall synthesis and requires RsgI's extracytoplasmic IDR. Intriguingly, the major peptidoglycan polymerase PBP1 also contains an extracytoplasmic IDR, and we show that this region is important for its function. Disparate IDRs can replace the native IDRs on both RsgI and PBP1, arguing that these unstructured regions function similarly. Our data support a model in which the RsgI–σI signaling system and PBP1 represent complementary pathways to repair gaps in the PG meshwork. The IDR on RsgI senses these gaps and activates σI, while the IDR on PBP1 directs the synthase to these sites to fortify them.
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