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Journal of Bacteriology, July 2006, p. 4715-4726, Vol. 188, No. 13
0021-9193/06/$08.00+0     doi:10.1128/JB.00351-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Erwinia carotovora Subspecies Produce Duplicate Variants of ExpR, LuxR Homologs That Activate rsmA Transcription but Differ in Their Interactions with N-Acylhomoserine Lactone Signals

Yaya Cui, Asita Chatterjee,* Hiroaki Hasegawa, and Arun K. Chatterjee

Division of Plant Sciences, University of Missouri, 108 Waters Hall, Columbia, Missouri 65211

Received 10 March 2006/ Accepted 12 April 2006

The N-acylhomoserine lactone (AHL) signaling system comprises a producing system that includes acylhomoserine synthase (AhlI, a LuxI homolog) and a receptor, generally a LuxR homolog. AHL controls exoprotein production in Erwinia carotovora and consequently the virulence for plants. In previous studies we showed that ExpR, a LuxR homolog, is an AHL receptor and that it activates transcription of rsmA, the gene encoding an RNA binding protein which is a global negative regulator of exoproteins and secondary metabolites. An unusual finding was that the transcriptional activity of ExpR was neutralized by AHL. We subsequently determined that the genomes of most strains of E. carotovora subspecies tested possess two copies of the expR gene: expR1, which was previously studied, and expR2, which was the focus of this study. Comparative analysis of the two ExpR variants of E. carotovora subsp. carotovora showed that while both variants activated rsmA transcription, there were significant differences in the patterns of their AHL interactions, the rsmA sequences to which they bound, and their relative efficiencies of activation of rsmA transcription. An ExpR2 mutant produced high levels of exoproteins and reduced levels of RsmA in the absence of AHL. This contrasts with the almost complete inhibition of exoprotein production and the high levels of RsmA production in an AhlI mutant that was ExpR1. Our results suggest that ExpR2 activity is responsible for regulating exoprotein production primarily by modulating the levels of an RNA binding protein.


* Corresponding author. Mailing address: Division of Plant Sciences, University of Missouri, 108 Waters Hall, Columbia, MO 65211. Phone: (573) 882-1892. Fax: (573) 882-0588. E-mail: chatterjeeas{at}missouri.edu.


Journal of Bacteriology, July 2006, p. 4715-4726, Vol. 188, No. 13
0021-9193/06/$08.00+0     doi:10.1128/JB.00351-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.




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