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Journal of Bacteriology, November 2004, p. 7456-7459, Vol. 186, No. 21
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.21.7456-7459.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The Aer Protein of Escherichia coli Forms a Homodimer Independent of the Signaling Domain and Flavin Adenine Dinucleotide Binding

Qinhong Ma,{dagger} Francis Roy, Sarah Herrmann, Barry L. Taylor, and Mark S. Johnson*

Division of Microbiology and Molecular Genetics, Loma Linda University, Loma Linda, California

Received 20 May 2004/ Accepted 4 August 2004

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.


* Corresponding author. Mailing address: Division of Microbiology and Molecular Genetics, Loma Linda University, Loma Linda, CA 92350. Phone: (909) 558-4480. Fax: (909) 558-4035. E-mail: mjohnson{at}som.llu.edu.

{dagger} Present address: Dow Chemical Company, San Diego, CA 92122.


Journal of Bacteriology, November 2004, p. 7456-7459, Vol. 186, No. 21
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.21.7456-7459.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.




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