The Aer protein of Escherichia coli forms a homodimer independent of the signaling domain and flavin adenine dinucleotide binding

被引：17

作者：

Ma, QH ^{[1
]}

Roy, F ^{[1
]}

Herrmann, S ^{[1
]}

Taylor, BL ^{[1
]}

Johnson, MS ^{[1
]}

机构：

[1] Loma Linda Univ, Div Microbiol & Mol Genet, Loma Linda, CA 92350 USA

来源：

JOURNAL OF BACTERIOLOGY | 2004年 / 186卷 / 21期

关键词：

D O I：

10.1128/JB.186.21.7456-7459.2004

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

In vivo cross-linking between native cysteines in the Aer receptor of Escherichia coli showed dimer formation at the membrane anchor and in the putative HAMP domain. Dimers also formed in mutants that did not bind flavin adenine dinucleotide and in truncated peptides without a signaling domain and part of the HAMP domain.

引用

页码：7456 / 7459

页数：4

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