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Journal of Bacteriology, September 2009, p. 5724-5733, Vol. 191, No. 18
0021-9193/09/$08.00+0     doi:10.1128/JB.01286-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Cellular Localization of Predicted Transmembrane and Soluble Chemoreceptors in Sinorhizobium meliloti{triangledown} ,{dagger}

Veronika M. Meier and Birgit E. Scharf*

Lehrstuhl für Genetik, Universität Regensburg, D-93040 Regensburg, Germany

Received 12 September 2008/ Accepted 6 July 2009

Bacterial chemoreceptors primarily locate in clusters at the cell pole, where they form large sensory complexes which recruit cytoplasmic components of the signaling pathway. The genome of the soil bacterium Sinorhizobium meliloti encodes seven transmembrane and two soluble chemoreceptors. We have investigated the localization of all nine chemoreceptors in vivo using genome-encoded fusions to a variant of the enhanced green fluorescent protein and to monomeric red fluorescent protein. Six of the transmembrane (McpT to McpX and McpZ) and both soluble (McpY and IcpA) receptors localize to the cell pole. Only McpS, encoded from the symbiotic plasmid pSymA, is evenly distributed in the cell. While the synthesis of all polar localized receptors is confined to exponential growth correlating with the motility phase of cells, McpS is only weakly expressed throughout cell culture growth. Therefore, motile S. meliloti cells form one major chemotaxis cluster that harbors all chemoreceptors except for McpS. Colocalization and deletion analysis demonstrated that formation of polar foci by the majority of receptors is dependent on other chemoreceptors and that receptor clusters are stabilized by the presence of the chemotaxis proteins CheA and CheW. The transmembrane McpV and the soluble IcpA localize to the pole independently of CheA and CheW. However, in mutant strains McpV formed delocalized polar caps that spread throughout the cell membrane while IcpA exhibited increased bipolarity. Immunoblotting of fractionated cells revealed that IcpA, which lacks any hydrophobic domains, nevertheless is associated to the cell membrane.

* Corresponding author. Present address: Biological Sciences, Life Sciences I, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061. Phone: (540) 231-0757. Fax: (540) 231-4043. E-mail: bscharf{at}vt.edu

{triangledown} Published ahead of print on 17 July 2009.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

Journal of Bacteriology, September 2009, p. 5724-5733, Vol. 191, No. 18
0021-9193/09/$08.00+0     doi:10.1128/JB.01286-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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