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Volume 160, Issue 5

NspS, a homologue of ABC-type periplasmic solute binding proteins, facilitates transduction of polyamine signals independent of their transport Free

Abstract

The polyamines norspermidine and spermidine are among the environmental signals that regulate 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 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 periplasmic ligand binding proteins may be widely utilized for sensory transduction.

  • Received:
  • Accepted:
  • Published Online:
Funding
This study was supported by the:
  • Appalachian State University Department of Biology
  • Office of Student Research and the Graduate Student Association
  • Senate at Appalachian State University
  • University Research Council
  • National Institute of Allergy and Infectious Disease
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2014-05-01
2024-04-26
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Vibrio cholerae NspS, a homologue of ABC-type periplasmic solute binding proteins, facilitates transduction of polyamine signals independent of their transport
Microbiology 160, 832 (2014); https://doi.org/10.1099/mic.0.075903-0
/content/journal/micro/10.1099/mic.0.075903-0
/content/journal/micro/10.1099/mic.0.075903-0
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