Membrane topology of the methyl-accepting chemotaxis protein DcrA fromDesulfovibrio vulgaris Hildenborough |
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Authors: | Harm M Deckers Gerrit Voordouw |
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Institution: | (1) Division of Biochemistry, Department of Biological Sciences, The University of Calgary, T2N 1N4 Calgary, Alberta, Canada |
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Abstract: | Alkaline phosphatase fusions were used to study the membrane topology of DcrA, a protein of 668 amino acids fromDesulfovibrio vulgaris Hildenborough, which has two potentially membrane-spanning hydrophobic sequences at residues 11 to 29 and 188 to 207. A fusion at amino acid residue 170 in the proposed periplasmic domain exhibited high alkaline phosphatase activity, while low activity was observed for a fusion at amino acid residue 284 in the proposed cytoplasmic domain. The data support a topological model for DcrA similar to that of the methyl-accepting chemotaxis proteins of the enteric bacteria. |
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Keywords: | alkaline phosphatase gene fusion Desulfovibrio chemotaxis DcrA |
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