Journal
MICROBIOLOGY-SGM
Volume 160, Issue -, Pages 832-843Publisher
MICROBIOLOGY SOC
DOI: 10.1099/mic.0.075903-0
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Funding
- Appalachian State University Department of Biology
- Office of Student Research at Appalachian State University
- Graduate Student Association Senate at Appalachian State University
- University Research Council
- National Institute of Allergy and Infectious Disease [AI096358]
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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.
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