Unknown

Dataset Information

0

Bacterial Haemoprotein Sensors of NO: H-NOX and NosP.


ABSTRACT: 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.

SUBMITTER: Bacon B 

PROVIDER: S-EPMC5659832 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature

altmetric image

Publications

Bacterial Haemoprotein Sensors of NO: H-NOX and NosP.

Bacon Bezalel B   Nisbett Lisa-Marie LM   Boon Elizabeth E  

Advances in microbial physiology 20170318


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 bact  ...[more]

Similar Datasets

| S-EPMC7290162 | biostudies-literature
| S-EPMC3819143 | biostudies-literature
| S-EPMC7356049 | biostudies-literature
| PRJNA728308 | ENA
| PRJNA389140 | ENA
| PRJNA754653 | ENA
| PRJNA304460 | ENA
| S-EPMC6217740 | biostudies-literature
| S-EPMC8921320 | biostudies-literature
| S-EPMC4465050 | biostudies-literature