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Identification of a region involved in the pheromone receptor function of the histidine kinase PlnB.

Johnsborg O, Godager LH, Nes IF

Laboratory of Microbial Gene Technology, Department of Chemistry and Biotechnology, Agricultural University of Norway, P.O. Box 5040, 1432 As, Norway. johnsborg@ikb.nlh.no

Bacteriocin biosynthesis in Lactobacillus plantarum is an inducible process, triggered by the secreted inducer peptide pheromone IP-C11. The environmental concentration of IP-C11 is monitored by the membrane-bound histidine protein kinase PlnB, which is part of a two-component signal transduction pathway. Upon interaction with IP-C11, PlnB phosphorylates the cognate response regulator PlnC. This regulator subsequently activates transcription of the bacteriocin genes. PlnB belongs to the HPK(10) subfamily of peptide-pheromone-activated histidine kinases. All members of this subfamily have an unusual polytopic membrane domain that previously has been shown to contain the peptide pheromone receptor. Employing an in vivo reporter assay, the present work investigated the receptor functionality of various mutagenized PlnB membrane domains. The results indicated that important determinants for receptor function locate to the most N-terminal extracytoplasmatic loop of the membrane domain. In addition, this region appears to be involved in the peptide pheromone interaction of ComD, another member of the HPK(10) subfamily.

Published 3 December 2004 in Arch Microbiol, 182(6): 450-7.
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