HAMP domain structural determinants for signalling and sensory adaptation in Tsr, theEscherichia coliserine chemoreceptor
نویسندگان
چکیده
منابع مشابه
HAMP domain structural determinants for signalling and sensory adaptation in Tsr, the Escherichia coli serine chemoreceptor.
HAMP domains mediate input-output transactions in many bacterial signalling proteins. To clarify the mechanistic logic of HAMP signalling, we constructed Tsr-HAMP deletion derivatives and characterized their steady-state signal outputs and sensory adaptation properties with flagellar rotation and receptor methylation assays. Tsr molecules lacking the entire HAMP domain or just the HAMP-AS2 heli...
متن کاملBiphasic control logic of HAMP domain signalling in the Escherichia coli serine chemoreceptor.
HAMP domains mediate input-output communication in many bacterial signalling proteins. To explore the dynamic bundle model of HAMP signalling (Zhou et al., Mol. Microbiol. 73: 801, 2009), we characterized the signal outputs of 118 HAMP missense mutants of the serine chemoreceptor, Tsr, by flagellar rotation patterns. Receptors with proline or charged amino acid replacements at critical hydropho...
متن کاملMutational analysis of the connector segment in the HAMP domain of Tsr, the Escherichia coli serine chemoreceptor.
HAMP domains are approximately 50-residue motifs, found in many bacterial signaling proteins, that consist of two amphiphilic helices joined by a nonhelical connector segment. The HAMP domain of Tsr, the serine chemoreceptor of Escherichia coli, receives transmembrane input signals from the periplasmic serine binding domain and in turn modulates output signals from the Tsr kinase control domain...
متن کاملThe tie that binds the dynamic duo: the connector between AS1 and AS2 in the HAMP domain of the Escherichia coli Tsr chemoreceptor.
A phospholipid bilayer membrane provides a selective permeability barrier that separates a cell’s world into “me” and “not me.” A large fraction of a bacterial genome is devoted to encoding proteins that allow only the desired molecules to breach this barrier and become concentrated in, or excluded from, the intracellular space. The membrane also filters information about the environment using ...
متن کاملFunctional suppression of HAMP domain signaling defects in the E. coli serine chemoreceptor.
HAMP domains play key signaling roles in many bacterial receptor proteins. The four-helix HAMP bundle of the homodimeric Escherichia coli serine chemoreceptor (Tsr) interacts with an adjoining four-helix sensory adaptation bundle to regulate the histidine autokinase CheA bound to the cytoplasmic tip of the Tsr molecule. The adaptation helices undergo reversible covalent modifications that tune ...
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ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 2013
ISSN: 0950-382X
DOI: 10.1111/mmi.12443