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J. Bacteriol. doi:10.1128/JB.01719-06
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Role of EAL containing proteins in multicellular behavior of Salmonella enterica serovar Typhimurium

Department of Microbiology, Tumor and Cell Biology (MTC), Karolinska Institutet, Box 280, SE-171 77 Stockholm, Sweden

^* To whom correspondence should be addressed. Email: ute.romling{at}ki.se.

	Abstract

GGDEF and EAL domain proteins are involved in the turnover of the novel secondary messenger cyclic-di(3'5')-guanylic acid (c-di-GMP) in many bacteria. The rdar morphotype, a multicellular behavior of Salmonella enterica serovar Typhimurium (S. Typhimurium) characterized by the expression of the extracellular matrix components cellulose and curli fimbriae is controlled by cyclic di-GMP. In this work the role of the EAL and GGDEF-EAL domain proteins on rdar morphotype development was investigated. Knock-out of four of 15 EAL and GGDEF-EAL domain proteins upregulated rdar morphotype expression; expression of CsgD, the central regulator of the rdar morphotype and, partially, cyclic di-GMP concentrations. More detailed analysis showed that the EAL domain protein STM4264 and the GGDEF-EAL domain protein STM1703, which highly upregulated the rdar morphotype, have overlapping, yet distinct functions. Another subset of EAL and GGDEF-EAL domain proteins influenced multicellular behavior in liquid culture and flagella mediated motility. Consequently, this work has shown that several EAL and GGDEF-EAL domain proteins, which act as phosphodiesterases, play a determinative role in the expression level of multicellular behavior of S. Typhimurium.

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