NosP Modulates Cyclic-di-GMP Signaling in Legionella pneumophila

被引:18
作者
Fischer, Jonathan T. [1 ,2 ]
Hossain, Sajjad [1 ,2 ]
Boon, Elizabeth M. [1 ,2 ]
机构
[1] SUNY Stony Brook, Dept Chem, Stony Brook, NY 11794 USA
[2] SUNY Stony Brook, Inst Chem Biol & Drug Discovery, Stony Brook, NY 11794 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
NITRIC-OXIDE REGULATION; H-NOX REGULATION; BIOFILM FORMATION; HISTIDINE KINASE; BINDING-PROTEIN; SENSOR KINASE; DIGUANYLATE; INSIGHTS; CO; PHOSPHODIESTERASE;
D O I
10.1021/acs.biochem.9b00618
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Biofilms form when bacteria adhere to a surface and secrete an extracellular polymeric substance. Bacteria embedded within a biofilm benefit from increased resistance to antibiotics, host immune responses, and harsh environmental factors. Nitric oxide (NO) is a signaling molecule that can modulate communal behavior, including biofilm formation, in many bacteria. In many cases, NO-induced biofilm dispersal is accomplished through signal transduction pathways that ultimately lead to a decrease in intracellular cyclic-di-GMP levels. H-NOX (heme nitric oxide/oxygen binding domain) proteins are the best characterized bacterial NO sensors and have been implicated in NO-mediated cyclic-di-GMP signaling, but we have recently discovered a second family of NO-sensitive proteins in bacteria named NosP (NO sensing protein); to date, a clear link between NosP signaling and cyclic-di-GMP metabolism has not been established. Here we present evidence that NosP (Lpg0279) binds to NO and directly affects cyclic-di-GMP production from two-component signaling proteins Lpg0278 and Lpg0277 encoded within the NosP operon. Lpg0278 and Lpg0277 are a histidine kinase and cyclic-di-GMP synthase/phosphodiesterase, respectively, that have already been established as being important in regulating Legionella pneumophila cyclic-di-GMP levels; NosP is thus implicated in regulating cyclic-di-GMP in L. pneumophila.
引用
收藏
页码:4325 / 4334
页数:10
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