PMID:22322964

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Citation

Shiba, Y, Miyagawa, H, Nagahama, H, Matsumoto, K, Kondo, D, Matsuoka, S, Matsumoto, K and Hara, H (2012) Exploring the relationship between lipoprotein mislocalisation and activation of the Rcs signal transduction system in Escherichia coli.Microbiology

Abstract

The Rcs phosphorelay signal transduction system controls genes for capsule production and many other envelope-related functions and is implicated in biofilm formation. We investigated the activation of the Rcs system in a pgsA null mutant of Escherichia coli, which completely lacks the major acidic phospholipids, phosphatidylglycerol and cardiolipin. We found that the Rcs activation, and consequent thermosensitivity, were suppressed by overexpression of the lgt gene encoding diacylglyceryltransferase, which catalyzes the modification of prolipoproteins that is the first step in the maturation and localisation process of lipoproteins and a prerequisite for the later steps. The outer membrane lipoprotein RcsF is an essential component of Rcs signalling. This lipoprotein was poorly localised to the outer membrane in the pgsA null mutant, probably because of the absence of phosphatidylglycerol, the major donor of diacylglycerol in the Lgt reaction. Even in pgsA(+) background the Rcs system was activated when RcsF was mislocalised to the inner membrane by alteration of the residues at position 2 and 3 of its mature form to inner membrane retention signals, or when it was mislocalised to the periplasm by fusing the mature form to maltose-binding protein. These results suggest that RcsF functions as a ligand for RcsC in activating Rcs signalling. Mislocalised versions of RcsF still responded to mutations pgsA, mdoH and tolB, further activating the Rcs system, but the rfaP mutation caused only slight activation. It seems that RcsF must be localised in the outer membrane to respond effectively to stimuli from outside of the cell.

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PubMed Online version:10.1099/mic.0.056945-0

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