Stony Brook University, Stony Brook, NY, United States.
Stony Brook University, Stony Brook, NY, United States.
Adv Microb Physiol. 2017;70:1-36. doi: 10.1016/bs.ampbs.2017.01.004. Epub 2017 Mar 18.
Low concentrations of nitric oxide (NO) modulate varied behaviours in bacteria including biofilm dispersal and quorum sensing-dependent light production. H-NOX (haem-nitric oxide/oxygen binding) is a haem-bound protein domain that has been shown to be involved in mediating these bacterial responses to NO in several organisms. However, many bacteria that respond to nanomolar concentrations of NO do not contain an annotated H-NOX domain. Nitric oxide sensing protein (NosP), a newly discovered bacterial NO-sensing haemoprotein, may fill this role. The focus of this review is to discuss structure, ligand binding, and activation of H-NOX proteins, as well as to discuss the early evidence for NO sensing and regulation by NosP domains. Further, these findings are connected to the regulation of bacterial biofilm phenotypes and symbiotic relationships.
低浓度的一氧化氮 (NO) 调节细菌的多种行为,包括生物膜分散和群体感应依赖性的光产生。H-NOX(血红素-一氧化氮/氧结合)是一种血红素结合蛋白结构域,已被证明在几种生物体中参与介导这些细菌对 NO 的反应。然而,许多对纳米摩尔浓度的 NO 有反应的细菌并不含有注释的 H-NOX 结构域。一氧化氮感应蛋白(NosP)是一种新发现的细菌一氧化氮感应血红素蛋白,可能可以填补这一角色。本综述的重点是讨论 H-NOX 蛋白的结构、配体结合和激活,以及讨论 NosP 结构域感应和调节 NO 的早期证据。此外,这些发现与细菌生物膜表型和共生关系的调节有关。