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Journal of Bacteriology, October 2005, p. 6770-6778, Vol. 187, No. 19
0021-9193/05/$08.00+0     doi:10.1128/JB.187.19.6770-6778.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Role of RcsF in Signaling to the Rcs Phosphorelay Pathway in Escherichia coli{dagger}

Nadim Majdalani,1,{ddagger} Michael Heck,2,{ddagger} Valerie Stout,2 and Susan Gottesman1*

Laboratory of Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892,1 School of Life Sciences, Arizona State University, Tempe, Arizona 85287-45012

Received 16 May 2005/ Accepted 18 July 2005

The rcs phosphorelay pathway components were originally identified as regulators of capsule synthesis. In addition to the transmembrane sensor kinase RcsC, the RcsA coregulator, and the response regulator RcsB, two new components have been characterized, RcsD and RcsF. RcsD, the product of the yojN gene, now renamed rcsD, acts as a phosphorelay between RcsC and RcsB. Transcription of genes for capsule synthesis (cps) requires both RcsA and RcsB; transcription of other promoters, including that for the small RNA RprA, requires only RcsB. RcsF was described as an alternative sensor kinase for RcsB. We have examined the role of RcsF in the activation of both the rprA and cps promoters. We find that a number of signals that lead to activation of the phosphorelay require both RcsF and RcsC; epistasis experiments place RcsF upstream of RcsC. The RcsF sequence is characteristic of lipoproteins, consistent with a role in sensing cell surface perturbation and transmitting this signal to RcsC. Activation of RcsF does not require increased transcription of the gene, suggesting that modification of the RcsF protein may act as an activating signal. Signals from RcsC require RcsD to activate RcsB. Sequencing of an rcsC allele, rcsC137, that leads to high-level constitutive expression of both cps and rprA suggests that the response regulator domain of RcsC plays a role in negatively regulating the kinase activity of RcsC. The phosphorelay and the variation in the activation mechanism (dependent upon or independent of RcsA) provide multiple steps for modulating the output from this system.

* Corresponding author. Mailing address: National Cancer Institute, 9000 Rockville Pike, Bldg. 37, Rm. 5132, Bethesda, MD 20892. Phone: (301) 496-3524. Fax: (301) 496-3875. E-mail: susang{at}helix.nih.gov.

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

{ddagger} These authors contributed equally to this work.

Journal of Bacteriology, October 2005, p. 6770-6778, Vol. 187, No. 19
0021-9193/05/$08.00+0     doi:10.1128/JB.187.19.6770-6778.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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