title: Vibrio cholerae NspS, a homologue of ABC-type periplasmic solute binding proteins, facilitates transduction of polyamine signals independent of their transport.
abstract: 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 periplasmic ligand binding proteins may be widely utilized for sensory transduction.
authors: Old Hickory Brewery, Hickory, NC 28601, USA.
authors: Steven R
authors: SR
authors: Cockerell
authors: Biomedical Sciences, The Medical University of South Carolina, Charleston, SC 29425, USA.
authors: Alex C
authors: AC
authors: Rutkovsky
authors: Department of Biochemistry and Biophysics, University of Chicago, Chicago, IL 60637, USA.
authors: Josiah P
authors: JP
authors: Zayner
authors: School of Biology, Georgia Institute of Technology, Atlanta, GA 30332, USA.
authors: Rebecca E
authors: RE
authors: Cooper
authors: Woodward Academy, College Park, GA 30337, USA.
authors: Lindsay R
authors: LR
authors: Porter
authors: Biomedical Sciences, Wake Forest University, Winston-Salem, NC 27157, USA.
authors: Sam S
authors: SS
authors: Pendergraft
authors: Department of Biological Sciences, Dartmouth College, Hanover, NH 03755, USA.
authors: Zach M
authors: ZM
authors: Parker
authors: Syngenta, Research Triangle Park, NC 27709, USA.
authors: Marcus W
authors: MW
authors: McGinnis
authors: Appalachian State University, Department of Biology, 572 Rivers St., Boone, NC 28608, USA.
authors: Ece
authors: E
authors: Karatan
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000378:metabolism*; D018441:Biofilms / Q000254:growth & development*; D006152:Cyclic GMP / Q000031:analogs & derivatives / Q000378:metabolism; D015398:Signal Transduction; D013095:Spermidine / Q000031:analogs & derivatives* / Q000378:metabolism*; D041242:Vibrio cholerae O139 / Q000187:drug effects* / Q000502:physiology*
chemical_list: D018528:ATP-Binding Cassette Transporters; C006760:norspermidine; C062025:bis(3',5')-cyclic diguanylic acid; D006152:Cyclic GMP; D013095:Spermidine