Abstract
Legionella pneumophila dot mutations cause defects in intracellular targeting 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 the mutations appear to be due to disrupted function of the predicted 1048-amino-acid residue DotA protein, and not by polarity effects on a downstream gene. Complementation studies indicated that the product of the dotA53 mutation results in a partially functional DotA protein, consistent with a stable N-terminal fragment having biological activity.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / genetics
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Base Sequence
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Cell Division / genetics
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Cell Line
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Cloning, Molecular
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DNA Primers / genetics
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DNA, Bacterial / genetics
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Genes, Bacterial*
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Genetic Complementation Test
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Genetic Linkage
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Humans
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Legionella pneumophila / genetics*
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Legionella pneumophila / growth & development*
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Legionella pneumophila / ultrastructure
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Macrophages / microbiology
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Microscopy, Electron
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Molecular Sequence Data
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Mutagenesis, Insertional
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Mutation*
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Open Reading Frames
Substances
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Bacterial Proteins
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DNA Primers
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DNA, Bacterial