ALTERED INTRACELLULAR TARGETING PROPERTIES ASSOCIATED WITH MUTATIONS IN THE LEGIONELLA-PNEUMOPHILA DOTA GENE

Legionella pneumophila dot mutations cause defects in intracellular ta rgeting of the microorganism within cultured macrophages. Each of the previously characterized dot mutations was shown to be complemented by a single open reading frame designated dotA. The defects caused by th e mutations appear to be due to disrupted function of the predicted 10 48-amino-acid residue DotA protein, and not by polarity effects on a d ownstream gene. Complementation studies indicated that the product of the dotA53 mutation results in a partially functional DotA protein, co nsistent with a stable N-terminal fragment having biological activity.