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Journal of Bacteriology, February 2003, p. 788-800, Vol. 185, No. 3
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.3.788-800.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

RmpA2, an Activator of Capsule Biosynthesis in Klebsiella pneumoniae CG43, Regulates K2 cps Gene Expression at the Transcriptional Level

Yi-Chyi Lai,1 Hwei-Ling Peng,2 and Hwan-You Chang1*

Department of Life Science and Institute of Molecular Medicine, National Tsing Hua University,1 Department of Biological Science and Technology, National Chiao Tung University, Hsin Chu, Taiwan, Republic of China2

Received 31 May 2002/ Accepted 5 November 2002

The rmpA2 gene, which encodes an activator for capsular polysaccharide (CPS) synthesis, was isolated from a 200-kb virulence plasmid of Klebsiella pneumoniae CG43. Based on the sequence homology with LuxR at the carboxyl-terminal DNA-binding motif, we hypothesized that RmpA2 exerts its effect by activating the expression of cps genes that are responsible for CPS biosynthesis. Two luxAB transcriptional fusions, each containing a putative promoter region of the K. pneumoniae K2 cps genes, were constructed and were found to be activated in the presence of multicopy rmpA2. The activation is likely due to direct binding of RmpA2 to the cps gene promoter through its C-terminal DNA binding motif. Moreover, the loss of colony mucoidy in a K. pneumoniae strain deficient in RcsB, a regulator for cps gene expression, could be recovered by complementing the strain with a multicopy plasmid carrying rmpA2. The CPS production in Lon protease-deficient K. pneumoniae significantly increased, and the effect was accompanied by an increase of RmpA2 stability. The expression of the rmpA2 gene was negatively autoregulated and could be activated when the organism was grown in M9 minimal medium. An IS3 element located upstream of the rmpA2 was required for the full activation of the rmpA2 promoter. In summary, our results suggest that the enhancement of K2 CPS synthesis in K. pneumoniae CG43 by RmpA2 can be attributed to its transcriptional activation of K2 cps genes, and the expression level of rmpA2 is autoregulated and under the control of Lon protease.

* Corresponding author. Mailing address: Department of Life Science, National Tsing Hua University, 101 Kuan-Fu Rd., 2nd Sec., Hsin Chu, Taiwan, Republic of China. Phone: 886-3-5742910. Fax: 886-3-5715934. E-mail: hychang{at}life.nthu.edu.tw.

Journal of Bacteriology, February 2003, p. 788-800, Vol. 185, No. 3
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.3.788-800.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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