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

Autor:	Francis Roy, Barry L. Taylor, Sarah Herrmann, Mark S. Johnson, Qinhong Ma
Rok vydání:	2004
Předmět:	Dimer Mutant Biology medicine.disease_cause Microbiology HAMP domain chemistry.chemical_compound Escherichia coli medicine Molecular Biology Flavin adenine dinucleotide Escherichia coli Proteins Gene Expression Regulation Bacterial Protein Structure Tertiary Flavin adenine dinucleotide binding B vitamins Cross-Linking Reagents chemistry Biochemistry Mutation Flavin-Adenine Dinucleotide Intercellular Signaling Peptides and Proteins Signal transduction Carrier Proteins Dimerization Signal Transduction
Zdroj:	Journal of Bacteriology. 186:7456-7459
ISSN:	1098-5530 0021-9193
DOI:	10.1128/jb.186.21.7456-7459.2004
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac9eb96c3160cf6029db92bbffaca8f8 https://doi.org/10.1128/jb.186.21.7456-7459.2004 Zobrazit plný text záznamu