Abstract
Rhizobium meliloti DctD is believed to have three functional domains: an N-terminal, two-component receiver domain; and like other sigma 54-dependent activators, C-terminal and central domains for DNA binding and transcription activation. We have characterized a progressive series of N-terminal deletions of R. meliloti DctD. The N-terminal domain was not needed for binding the dctA upstream activation sequence. Only 25% of the C-terminal end of the receive domain was needed to significantly inhibit the central domain, and proteins lacking up to 60% of the N-terminal end of the receiver domain were 'inducible' in R. meliloti cells. We hypothesize that the N-terminal two-thirds of the DctD receiver domain augments and controls an adjacent subdomain for inhibiting the central domain.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bacterial Proteins*
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Binding Sites
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Carrier Proteins / biosynthesis
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Carrier Proteins / genetics
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DNA, Bacterial / metabolism
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Dicarboxylic Acid Transporters*
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Genes, Synthetic
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Models, Chemical
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Phosphorylation
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Promoter Regions, Genetic
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Protein Kinases / genetics
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Protein Kinases / physiology*
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Protein Processing, Post-Translational
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Protein Structure, Tertiary*
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Receptors, Cell Surface / genetics
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Receptors, Cell Surface / physiology*
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Recombinant Fusion Proteins / metabolism
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Sigma Factor / physiology*
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Signal Transduction
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Sinorhizobium meliloti / genetics
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Sinorhizobium meliloti / physiology*
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Transcription Factors / chemistry
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Transcription Factors / physiology*
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Transcription, Genetic
Substances
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Bacterial Proteins
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Carrier Proteins
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DNA, Bacterial
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Dicarboxylic Acid Transporters
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Receptors, Cell Surface
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Recombinant Fusion Proteins
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Sigma Factor
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Transcription Factors
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dctA protein, Sinorhizobium meliloti
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DCTB protein, Sinorhizobium
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dctD protein, Rhizobium meliloti
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Protein Kinases