A noncanonical cytochrome c stimulates calcium binding by PilY1 for type IVa pili formation.
A noncanonical cytochrome c stimulates calcium binding by PilY1 for type IVa pili formation.
复制标题
DOI：
10.1073/pnas.2115061119
复制
发表时间：
2022-02-08
影响因子：
11.1
通讯作者：
Søgaard-Andersen L
中科院分区：
文献类型：
--
作者：
Herfurth M;Treuner-Lange A;Glatter T;Wittmaack N;Hoiczyk E;Pierik AJ;Søgaard-Andersen L
Ⅳ a型皮利（T4 aP）是在不同环境条件下起作用的细菌表面结构。在用于T4 aP形成的机器中，次要菌毛蛋白和PilY 1的复合物引发T4 aP形成，并且还存在于菌毛尖端介导粘附。与其他几种细菌粘附素类似，PilY 1依赖于钙结合功能。在这里，我们证明，在粘球菌xanthus，PilY 1在低水平的钙依赖于辅助蛋白TfcP结合钙，从而稳定的蛋白质。TfcP是一种不参与电子传递的非典型细胞色素c。相反，我们的数据支持TfcP与PilY 1瞬时相互作用以刺激钙结合。通过这种方式，TfcP扩大了T4 aP发挥作用的钙水平范围。IVa型皮利（T4 aP）是多功能的细菌细胞表面结构，其经历由跨越细胞壁的T4 aP机器提供动力的延伸/粘附/收缩循环。在该机器中，由四个次要菌毛蛋白和PilY 1组成的复合物引发T4 aP延伸，并且也存在于菌毛尖端介导粘附。与许多其他细菌类似，黄色粘球菌含有多个未完全了解的次要菌毛蛋白/PilY 1集。在这里，我们报告说，未成年人的菌毛蛋白和PilY 1（PilY1.1）的cluster_1形式启动和尖端复合物的钙和非典型的细胞色素c（TfcP）与一个不寻常的His/Cys血红素连接。我们提供的证据表明，TfcP不太可能参与电子传递，而是在低钙浓度下刺激PilY1.1与钙结合，从而稳定PilY1.1并使T4 aP在更广泛的钙浓度范围内发挥作用。这些结果不仅确定了一个以前未描述的功能的细胞色素c，但也说明了如何纳入一个辅助因素扩大了环境范围下的T4 aP系统的功能。
Type IVa pili (T4aP) are bacterial surface structures that function under different environmental conditions. In the machine for T4aP formation, a complex of minor pilins and PilY1 primes T4aP formation and is also present at the pilus tip mediating adhesion. Similar to several other bacterial adhesins, PilY1 depends on calcium binding for function. Here, we demonstrate that in Myxococcus xanthus, PilY1 at low levels of calcium depends on the accessory protein TfcP to bind calcium, thereby stabilizing the protein. TfcP is a noncanonical cytochrome c that does not participate in electron transport. Rather our data support that TfcP interacts transiently with PilY1 to stimulate calcium binding. In this way, TfcP expands the range of calcium levels under which T4aP functions. Type IVa pili (T4aP) are versatile bacterial cell surface structures that undergo extension/adhesion/retraction cycles powered by the cell envelope–spanning T4aP machine. In this machine, a complex composed of four minor pilins and PilY1 primes T4aP extension and is also present at the pilus tip mediating adhesion. Similar to many several other bacteria, Myxococcus xanthus contains multiple minor pilins/PilY1 sets that are incompletely understood. Here, we report that minor pilins and PilY1 (PilY1.1) of cluster_1 form priming and tip complexes contingent on calcium and a noncanonical cytochrome c (TfcP) with an unusual His/Cys heme ligation. We provide evidence that TfcP is unlikely to participate in electron transport and instead stimulates calcium binding by PilY1.1 at low-calcium concentrations, thereby stabilizing PilY1.1 and enabling T4aP function in a broader range of calcium concentrations. These results not only identify a previously undescribed function of cytochromes c but also illustrate how incorporation of an accessory factor expands the environmental range under which the T4aP system functions.
登录
查看更多内容
影响因子：
5.2
作者：
Kracke F;Vassilev I;Krömer JO
通讯作者：
Krömer JO
DOI：
10.1126/science.aad2001
发表时间：
2016-03-11
期刊：
Science (New York, N.Y.)
影响因子：
--
作者：
Chang YW;Rettberg LA;Treuner-Lange A;Iwasa J;Søgaard-Andersen L;Jensen GJ
通讯作者：
Jensen GJ
影响因子：
3.1
作者：
Cheng, Yuan;Johnson, Michael D. L.;Thomas, Christopher E.
通讯作者：
Thomas, Christopher E.
影响因子：
5.7
作者：
Hoppe J;Ünal CM;Thiem S;Grimpe L;Goldmann T;Gaßler N;Richter M;Shevchuk O;Steinert M
通讯作者：
Steinert M
影响因子：
3.2
作者：
Friedrich, Carmen;Bulyha, Iryna;Sogaard-Andersen, Lotte
通讯作者：
Sogaard-Andersen, Lotte