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Dual specificity of a prokaryotic GTPase‐activating protein (GAP) to two small Ras‐like GTPases in Myxococcus xanthus
The FEBS Journal ( IF 5.5 ) Pub Date : 2020-08-08 , DOI: 10.1111/febs.15513 Manil Kanade 1 , Ningthoujam Birjeet Singh 1 , Sonal Lagad 1 , Jyoti Baranwal 1 , Pananghat Gayathri 1
The FEBS Journal ( IF 5.5 ) Pub Date : 2020-08-08 , DOI: 10.1111/febs.15513 Manil Kanade 1 , Ningthoujam Birjeet Singh 1 , Sonal Lagad 1 , Jyoti Baranwal 1 , Pananghat Gayathri 1
Affiliation
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Two small Ras‐like GTPases, MglA and SofG, work in synchrony to drive cell polarity and motility in the soil bacterium, Myxococcus xanthus. While MglA regulates two types of motility in Myxococcus and drives cell polarity reversals, SofG regulates social motility enabled by the type IV pili (T4P) machinery. In order to understand the molecular basis of how multiple GTPases act concertedly, we initiated biochemical studies on SofG. A construct of SofG (SofG∆60) was purified as a homogenous monomer and could bind to GDP and GTP. Intrinsic GTP hydrolysis by SofG∆60 was negligible. Earlier work from the laboratory revealed that MglB functions both as a GTPase‐activating protein (GAP) and a guanine nucleotide exchange factor (GEF) for MglA. Biochemical assays of SofG∆60 established that MglB interacts with GTP‐bound SofG∆60 and acts as a GAP for SofG∆60. Interaction of MglB with SofG∆60 in the GDP‐bound conformation was not observed, thereby suggesting that MglB might not act as a GEF for SofG∆60. The existence of a common GAP for both SofG and MglA could potentially contribute to concerted regulation of their GTPase activities, and mediate crosstalk between the two GTPases involved in motility of M. xanthus. Sequence analysis revealed the features for a SofG‐like subclass of prokaryotic small Ras‐like GTPases that enable MglB to act as a dual‐specificity GAP.
中文翻译：
原核GTP酶激活蛋白（GAP）对黄色粘球菌中两个小的Ras样GTP酶的双重特异性
两个小的Ras-GTP酶一样，MGLA和SofG，同步工作在土壤细菌，驱动细胞极性和运动粘细菌。MglA调节粘球菌中的两种运动并驱动细胞极性逆转，而SofG则通过IV型菌毛（T4P）机制调节社交运动。为了了解多个GTPases如何协同作用的分子基础，我们启动了SofG的生化研究。SofG（SofG ∆60）的构建体被纯化为同质单体，可以与GDP和GTP结合。SofG ∆60导致的内在GTP水解可以忽略不计。实验室的早期工作表明，MglB既可充当MglA的GTP酶激活蛋白（GAP），又可用作鸟嘌呤核苷酸交换因子（GEF）。SofG的生化测定Δ60确立MglB与GTP结合的SofG相互作用Δ60和充当SofG一个GAP Δ60。未观察到MglB与SofG ∆60在GDP结合构象中的相互作用，因此表明MglB可能不充当SofG ∆60的GEF 。SofG和MglA的共同GAP的存在可能有助于其GTPase活性的协调调节，并介导参与黄原体运动的两个GTPases之间的串扰。。序列分析揭示了原核小类Ras样GTPases的SofG样亚类的功能，使MglB可以充当双重特异性GAP。
更新日期：2020-08-08
中文翻译：
原核GTP酶激活蛋白（GAP）对黄色粘球菌中两个小的Ras样GTP酶的双重特异性
两个小的Ras-GTP酶一样，MGLA和SofG，同步工作在土壤细菌，驱动细胞极性和运动粘细菌。MglA调节粘球菌中的两种运动并驱动细胞极性逆转，而SofG则通过IV型菌毛（T4P）机制调节社交运动。为了了解多个GTPases如何协同作用的分子基础，我们启动了SofG的生化研究。SofG（SofG ∆60）的构建体被纯化为同质单体，可以与GDP和GTP结合。SofG ∆60导致的内在GTP水解可以忽略不计。实验室的早期工作表明，MglB既可充当MglA的GTP酶激活蛋白（GAP），又可用作鸟嘌呤核苷酸交换因子（GEF）。SofG的生化测定Δ60确立MglB与GTP结合的SofG相互作用Δ60和充当SofG一个GAP Δ60。未观察到MglB与SofG ∆60在GDP结合构象中的相互作用，因此表明MglB可能不充当SofG ∆60的GEF 。SofG和MglA的共同GAP的存在可能有助于其GTPase活性的协调调节，并介导参与黄原体运动的两个GTPases之间的串扰。。序列分析揭示了原核小类Ras样GTPases的SofG样亚类的功能，使MglB可以充当双重特异性GAP。
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