1887

Abstract

The ATP-dependent Lon (La) protease is ubiquitous in nature and regulates a diverse set of physiological responses in bacteria. In this paper a mutant of the -proteobacterium C58 has been characterized. Unlike mutants of , the mutant of grows very slowly, is not filamentous and exhibits normal resistance to UV irradiation. The mutant retains motility and chemotaxis, produces apparently normal amounts of exopolysacchride, but displays severe defects in cell morphology, with 80 % of the mutant cells appearing Y-shaped. Lon protease of shares high homology with its counterparts in and in , and functionally complements an mutant for defects in morphology and RcsA-mediated regulation of capsular polysaccharide production. Mutations at sites of Lon corresponding to the ATP-binding site and the active site serine of the Lon protease abolish complementation of phenotypes of the and mutants. The nucleotide sequence upstream of contains an element similar to the consensus heat-shock promoter of . Northern and Western blot analyses indicated that expression of is induced by elevated temperature, albeit to a much lower level than that of . The mutant is highly attenuated for virulence, suggesting that Lon may be required for the proper expression, assembly or function of the VirB/D4-mediated T-DNA transfer system.

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2006-04-01
2024-04-19
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