Lon protease of the α-proteobacterium Agrobacterium tumefaciens is required for normal growth, cellular morphology and full virulence

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Abstract
The ATP-dependent Lon (La) protease is ubiquitous in nature and regulates a diverse set of physiological responses in bacteria. In this paper alonmutant of theα-proteobacteriumAgrobacterium tumefaciensC58 has been characterized. Unlikelonmutants ofEscherichia coli, thelonmutant ofA. tumefaciensgrows 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 ofA. tumefaciensshares high homology with its counterparts inE. coliand inSinorhizobium meliloti, and functionally complements anE. coli lonmutant for defects in morphology and RcsA-mediated regulation of capsular polysaccharide production. Mutations at sites of LonAtcorresponding to the ATP-binding site and the active site serine of theE. coliLon protease abolish complementation of phenotypes of theA. tumefaciensandE. coli lonmutants. The nucleotide sequence upstream ofA. tumefaciens loncontains an element similar to the consensusσ32heat-shock promoter ofE. coli. Northern and Western blot analyses indicated that expression oflonis induced by elevated temperature, albeit to a much lower level than that ofgroEL. Thelonmutant 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.