Abstract
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.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Carrier Proteins / chemistry*
-
Carrier Proteins / metabolism*
-
Cross-Linking Reagents
-
Dimerization
-
Escherichia coli / genetics
-
Escherichia coli / metabolism*
-
Escherichia coli Proteins / chemistry*
-
Escherichia coli Proteins / metabolism*
-
Flavin-Adenine Dinucleotide / metabolism*
-
Gene Expression Regulation, Bacterial
-
Intercellular Signaling Peptides and Proteins
-
Mutation
-
Protein Structure, Tertiary
-
Signal Transduction
Substances
-
Aer protein, E coli
-
Carrier Proteins
-
Cross-Linking Reagents
-
Escherichia coli Proteins
-
Intercellular Signaling Peptides and Proteins
-
Flavin-Adenine Dinucleotide