Vibrio cholerae NspS, a homologue of ABC-type periplasmic solute binding proteins, facilitates transduction of polyamine signals independent of their transport
Vibrio cholerae NspS, a homologue of ABC-type periplasmic solute binding proteins, facilitates transduction of polyamine signals independent of their transport
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DOI：
10.1099/mic.0.075903-0
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发表时间：
2014-05-01
期刊：
影响因子：
2.8
通讯作者：
Karatan, Ece
中科院分区：
文献类型：
--
作者：
Cockerell, Steven R.;Rutkovsky, Alex C.;Karatan, Ece
多胺、去甲精胺和亚精胺是调节霍乱弧菌生物膜形成的环境信号之一。这些多胺的作用是由NSPS介导的，NSPS是细菌周质溶质结合蛋白超家族的成员。到目前为止，这个超家族的几乎所有成员都是参与营养吸收的ATP结合盒类型转运体的组成部分。因此，在目前对霍乱弧菌基因组的注释中，NSPS被赋予了运输功能。这项研究的目的是进一步描述NSPS的特征，并调查其在运输中的潜在作用。我们的结果支持NSPS在响应去甲精胺和亚精胺的信号转导中的作用，但不支持它们的转运。此外，我们提供的证据表明，这些多胺信号是由细胞内的c-di-GMP信号网络处理的。此外，我们提供了比较基因组学分析，揭示了NSPS样蛋白在各种细菌中的存在，表明周质粒配体结合蛋白可能被广泛用于感觉转导。
The polyamines norspermidine and spermidine are among the environmental signals that regulate Vibrio cholerae biofilm formation. The effects of these polyamines are mediated by NspS, a member of the bacterial periplasmic solute binding protein superfamily. Almost all members of this superfamily characterized to date are components of ATP-binding cassette-type transporters involved in nutrient uptake. Consequently, in the current annotation of the V. cholerae genome, NspS has been assigned a function in transport. The objective of this study was to further characterize NspS and investigate its potential role in transport. Our results support a role for NspS in signal transduction in response to norspermidine and spermidine, but not their transport. In addition, we provide evidence that these polyamine signals are processed by c-di-GMP signalling networks in the cell. Furthermore, we present comparative genomics analyses which reveal the presence of NspS-like proteins in a variety of bacteria, suggesting that periplasnnic ligand binding proteins may be widely utilized for sensory transduction.