The Aer protein of Escherichia coli forms a homodimer independent of the signaling domain and flavin adenine dinucleotide binding.
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.
Division of Microbiology and Molecular Genetics, Loma Linda University, Loma Linda, CA 92350, USA. mjohnson@som.llu.edu
Qinhong
Q
Ma
Francis
F
Roy
Sarah
S
Herrmann
Barry L
BL
Taylor
Mark S
MS
Johnson
D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism*; D003432:Cross-Linking Reagents; D019281:Dimerization; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D036341:Intercellular Signaling Peptides and Proteins; D009154:Mutation; D017434:Protein Structure, Tertiary; D015398:Signal Transduction
C108679:Aer protein, E coli; D002352:Carrier Proteins; D003432:Cross-Linking Reagents; D029968:Escherichia coli Proteins; D036341:Intercellular Signaling Peptides and Proteins; D005182:Flavin-Adenine Dinucleotide