TY - JOUR
T1 - The Aer protein of Escherichia coli forms a homodimer independent of the signaling domain and flavin adenine dinucleotide binding
AU - Ma, Qinhong
AU - Roy, Francis
AU - Herrmann, Sarah
AU - Taylor, Barry L.
AU - Johnson, Mark S.
N1 - The Escherichia coli energy-sensing Aer protein initiates aerotaxis towards environments supporting optimal cellular energy. The Aer sensor is an N-terminal, FAD-binding, PAS domain. The PAS domain is linked by an F1 region to a membrane anchor, and in the C-terminal half of Aer, a HAMP domain links the membrane anchor to the signaling domain.
PY - 2004/11
Y1 - 2004/11
N2 - 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.
AB - 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.
KW - Protein Structure, Tertiary
KW - Carrier Proteins/chemistry
KW - Cross-Linking Reagents
KW - Flavin-Adenine Dinucleotide/metabolism
KW - Signal Transduction
KW - Escherichia coli Proteins/chemistry
KW - Intercellular Signaling Peptides and Proteins
KW - Mutation
KW - Escherichia coli/genetics
KW - Gene Expression Regulation, Bacterial
KW - Dimerization
UR - https://www.scopus.com/pages/publications/6044247517
UR - https://www.scopus.com/pages/publications/6044247517#tab=citedBy
U2 - 10.1128/JB.186.21.7456-7459.2004
DO - 10.1128/JB.186.21.7456-7459.2004
M3 - Article
C2 - 15489458
SN - 0021-9193
VL - 186
SP - 7456
EP - 7459
JO - Journal of Bacteriology
JF - Journal of Bacteriology
IS - 21
ER -