MEMBRANE TOPOLOGY OF THE METHYL-ACCEPTING CHEMOTAXIS PROTEIN DCRA FROM DESULFOVIBRIO-VULGARIS HILDENBOROUGH

被引：9

作者：

DECKERS, HM

VOORDOUW, G

机构：

[1] Division of Biochemistry, Department of Biological Sciences, The University of Calgary, Calgary, T2N 1N4, Alberta

来源：

ANTONIE VAN LEEUWENHOEK INTERNATIONAL JOURNAL OF GENERAL AND MOLECULAR MICROBIOLOGY | 1994年 / 65卷 / 01期

关键词：

ALKALINE PHOSPHATASE; GENE FUSION; DESULFOVIBRIO; CHEMOTAXIS; DCRA;

D O I：

10.1007/BF00878273

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Alkaline phosphatase fusions were used to study the membrane topology of DcrA, a protein of 668 amino acids from Desulfovibrio 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.

引用

页码：7 / 12

页数：6

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