Structure-Function Relationships in the HAMP and Proximal Signaling Domains of the Aerotaxis Receptor Aer
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چکیده
منابع مشابه
Structure-function relationships in the HAMP and proximal signaling domains of the aerotaxis receptor Aer.
Aer, the Escherichia coli aerotaxis receptor, faces the cytoplasm, where the PAS (Per-ARNT-Sim)-flavin adenine dinucleotide (FAD) domain senses redox changes in the electron transport system or cytoplasm. PAS-FAD interacts with a HAMP (histidine kinase, adenylyl cyclase, methyl-accepting protein, and phosphatase) domain to form an input-output module for Aer signaling. In this study, the struct...
متن کاملInteractions between the PAS and HAMP domains of the Escherichia coli aerotaxis receptor Aer.
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. The F1 region, membrane anchor, and HAMP domain are...
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The Escherichia coli Aer protein contains an N-terminal PAS domain that binds flavin adenine dinucleotide (FAD), senses aerotactic stimuli, and communicates with the output signaling domain. To explore the roles of the intervening F1 and HAMP segments in Aer signaling, we isolated plasmid-borne aerotaxis-defective mutations in a host strain lacking all chemoreceptors of the methyl-accepting che...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 2008
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.01858-07