Phosphorylation of Bacillus subtilis gene regulator AbrB modulates its DNA-binding properties
Phosphorylation of Bacillus subtilis gene regulator AbrB modulates its DNA-binding properties
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DOI：
10.1111/mmi.12617
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发表时间：
2014-06-01
影响因子：
3.6
通讯作者：
Mijakovic, Ivan
中科院分区：
文献类型：
--
作者：
Kobir, Ahasanul;Poncet, Sandrine;Mijakovic, Ivan
AbrB是枯草芽孢杆菌中参与过渡相现象的全局基因调节因子。它参与了一个复杂的监管网络管理的表达固定阶段的功能。先前发现AbrB在靠近其C-末端寡聚化结构域的丝氨酸86上被磷酸化。本文报道了Abr B可以被三个B磷酸化。在过渡期和稳定期表达的枯草杆菌丝氨酸/苏氨酸激酶：PrkC、PrkD和YabT。我们的体外研究结果表明，AbrB磷酸化阻碍其DNA结合，并取消结合协同性。在体内，我们建立了一个磷酸模拟突变abrB S86 D导致显着的损失AbrB控制几个关键的目标功能：外切蛋白酶的生产，能力的发展和孢子形成。对abrBS 86 D和S86 A突变株的更广泛的转录组分析揭示了大量靶基因的失调。因此，我们建议，AbrB磷酸化作为一个额外的输入微调的活性，这ambiactive基因调节。
AbrB is a global gene regulator involved in transition phase phenomena in Bacillus subtilis. It participates in a complex regulatory network governing the expression of stationary-phase functions. AbrB was previously found to be phosphorylated on serine 86 located close to its C-terminal oligomerization domain. Here we report that AbrB can be phosphorylated by three B. subtilis serine/threonine kinases expressed during the transition and stationary phase: PrkC, PrkD and YabT. Our in vitro findings suggest that AbrB phosphorylation impedes its DNA binding and abolishes binding cooperativity. In vivo we established that a phospho-mimetic mutation abrB S86D leads to a significant loss of AbrB control over several key target functions: exoprotease production, competence development and sporulation. A wider transcriptome analysis of abrBS86D and S86A mutant strains revealed deregulation of a large number of target genes. We therefore propose that AbrB phosphorylation serves as an additional input for fine-tuning the activity of this ambiactive gene regulator.