Mutational analysis reveals functional similarity between NARX, a nitrate sensor in Escherichia coli K-12, and the methyl-accepting chemotaxis proteins.
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Mutations in the molybdenum cofactor biosynthetic protein Cnx1G from Arabidopsis thaliana define functions for molybdopterin binding, molybdenum insertion, and molybdenum cofactor stabilizationStructural characterization of AS1–membrane interactions from a subset of HAMP domainsThe YfiBNR signal transduction mechanism reveals novel targets for the evolution of persistent Pseudomonas aeruginosa in cystic fibrosis airwaysGenetic analysis of the HAMP domain of the Aer aerotaxis sensor localizes flavin adenine dinucleotide-binding determinants to the AS-2 helix.The S helix mediates signal transmission as a HAMP domain coiled-coil extension in the NarX nitrate sensor from Escherichia coli K-12.Functional similarities among two-component sensors and methyl-accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmembrane signal transduction.The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins.A cytoplasmic coiled-coil domain is required for histidine kinase activity of the yeast osmosensor, SLN1.Aerobic activity of Escherichia coli alcohol dehydrogenase is determined by a single amino acidMutational analysis of a conserved signal-transducing element: the HAMP linker of the Escherichia coli nitrate sensor NarXProbing conservation of HAMP linker structure and signal transduction mechanism through analysis of hybrid sensor kinases.Nitrate- and nitrite-sensing protein NarX of Escherichia coli K-12: mutational analysis of the amino-terminal tail and first transmembrane segmentTransduction of envelope stress in Escherichia coli by the Cpx two-component system.Computational learning reveals coiled coil-like motifs in histidine kinase linker domainsDual response regulators (NarL and NarP) interact with dual sensors (NarX and NarQ) to control nitrate- and nitrite-regulated gene expression in Escherichia coli K-12Transmembrane signalling by a hybrid protein: communication from the domain of chemoreceptor Trg that recognizes sugar-binding proteins to the kinase/phosphatase domain of osmosensor EnvZ.Localization of upstream sequence elements required for nitrate and anaerobic induction of fdn (formate dehydrogenase-N) operon expression in Escherichia coli K-12Functions of the gene products of Escherichia coli.Either of two functionally redundant sensor proteins, NarX and NarQ, is sufficient for nitrate regulation in Escherichia coli K-12.Interactions between the PAS and HAMP domains of the Escherichia coli aerotaxis receptor Aer.Mutationally altered signal output in the Nart (NarX-Tar) hybrid chemoreceptor.Attractant- and disulfide-induced conformational changes in the ligand binding domain of the chemotaxis aspartate receptor: a 19F NMR study.Screening and quantification of the expression of antibiotic resistance genes in Acinetobacter baumannii with a microarray.New combinations of mutations in VanD-Type vancomycin-resistant Enterococcus faecium, Enterococcus faecalis, and Enterococcus avium strains.Five residues in the HtrI transducer membrane-proximal domain close the cytoplasmic proton-conducting channel of sensory rhodopsin I.A NarX-Tar chimera mediates repellent chemotaxis to nitrate and nitrite.
P2860
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P2860
Mutational analysis reveals functional similarity between NARX, a nitrate sensor in Escherichia coli K-12, and the methyl-accepting chemotaxis proteins.
description
1992 nî lūn-bûn
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1992年の論文
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1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
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1992年论文
@zh-cn
name
Mutational analysis reveals fu ...... accepting chemotaxis proteins.
@ast
Mutational analysis reveals fu ...... accepting chemotaxis proteins.
@en
type
label
Mutational analysis reveals fu ...... accepting chemotaxis proteins.
@ast
Mutational analysis reveals fu ...... accepting chemotaxis proteins.
@en
prefLabel
Mutational analysis reveals fu ...... accepting chemotaxis proteins.
@ast
Mutational analysis reveals fu ...... accepting chemotaxis proteins.
@en
P2093
P2860
P1476
Mutational analysis reveals fu ...... accepting chemotaxis proteins.
@en
P2093
P2860
P304
P356
10.1128/JB.174.11.3667-3675.1992
P407
P577
1992-06-01T00:00:00Z