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J. Bacteriol. doi:10.1128/JB.01170-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The two-component regulatory system TCS08 is involved in cellobiose metabolism of Streptococcus pneumoniae R6

Department of Microbiology, University of Kaiserslautern, Paul Ehrlich Strasse 23, D-67663 Kaiserslautern, Germany

^* To whom correspondence should be addressed. Email: hakenb{at}rhrk.uni-kl.de.

	Abstract

The two-component system TCS08 is one of the regulatory systems that is important for virulence of Streptococcus pneumoniae. In order to investigate the TCS08 regulon we have analyzed transcription profiles of mutants derived from S. pneumoniae R6 by microarray analysis. Since deletion mutants are often without a significant phenotype, a mutation in the histidine kinase HK08 was constructed, T133P, in analogy to the phosphatase mutation T230P in the H-box of the S. pneumoniae CiaH kinase described recently (43). In addition, a deletion mutant was constructed in rr08 encoding the cognate response regulator. The most heavily suppressed genes in the hk08 mutant were spr0276-spr0282 encoding a putative cellobiose phosphoenolpyruvate sugar phosphotransferase system (PTS). Whereas the R6 Sm^R parent strain and the rr08 mutant readily grew on cellobiose, the hk08 mutant and selected deletion mutants in the PTS cluster did not, strongly suggesting that TCS08 is involved in the catabolism of cellobiose. Homologues of the TCS08 system were found in closely related streptococci and other Gram positive cocci. However, the genes spr0276 - spr0282 encoding the putative cellobiose PTS system represent a genomic island in S. pneumoniae and homologues were found in S. gordonii only, suggesting that it might contribute to the pathogenicity potential of the pneumococcus.

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