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Journal of Bacteriology, June 2009, p. 3639-3648, Vol. 191, No. 11
0021-9193/09/$08.00+0 doi:10.1128/JB.00009-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Guangxi Key Laboratory of Subtropical Bioresources Conservation and Utilization, The Key Laboratory of Ministry of Education for Microbial and Plant Genetic Engineering, and College of Life Science and Technology, Guangxi University, 100 Daxue Road, Nanning, Guangxi 530004, China
Received 5 January 2009/ Accepted 23 March 2009
Adenosine kinase (ADK) is a purine salvage enzyme and a typical housekeeping enzyme in eukaryotes which catalyzes the phosphorylation of adenosine to form AMP. Since prokaryotes synthesize purines de novo and no endogenous ADK activity is detectable in Escherichia coli, ADK has long been considered to be rare in bacteria. To date, only two prokaryotes, both of which are gram-positive bacteria, have been reported to contain ADK. Here we report that the gram-negative bacterium Xanthomonas campestris pathovar campestris, the causal agent of black rot of crucifers, possesses a gene (designated adkXcc) encoding an ADK (named ADKXcc), and we demonstrate genetically that the ADKXcc is involved in extracellular polysaccharide (EPS) production, cell motility, and pathogenicity of X. campestris pv. campestris. adkXcc was overexpressed as a His6-tagged protein in E. coli, and the purified His6-tagged protein exhibited ADK activity. Mutation of adkXcc did not affect bacterial growth in rich and minimal media but led to an accumulation of intracellular adenosine and diminutions of intracellular ADK activity and ATP level, as well as EPS. The adkXcc mutant displayed significant reductions in bacterial growth and virulence in the host plant.
Published ahead of print on 27 March 2009.
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