Membrane topology of the methyl-accepting chemotaxis protein DcrA fromDesulfovibrio vulgaris Hildenborough
- 1 January 1994
- journal article
- research article
- Published by Springer Nature in Antonie van Leeuwenhoek
- Vol. 65 (1) , 7-12
- https://doi.org/10.1007/bf00878273
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.Keywords
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