Transmembrane signaling in chimeras of the Escherichia coli aspartate and serine chemotaxis receptors and bacterial class III adenylyl cyclases

Journal of Biological Chemistry

Volumn 285, Issue 3, 2010, Pages 2090-2099

  Kanchan, Kajal ^a   Linder, Jürgen ^a   Winkler, Karin ^a   Hantke, Klaus ^a   Schultz, Anita ^a   Schultz, Joachim E ^a  

^a UNIVERSITY OF TÜBINGEN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ARTHROSPIRA PLATENSIS; ASPARTATES; CHEMICAL SENSING; CO-EXPRESSION; CYCLASES; HOMODIMERIZATION; IN-VITRO; L-SERINE; LIGAND BINDING; MEMBRANE ANCHORS; MICROMOLAR CONCENTRATION; MOLECULAR ARCHITECTURE; MYCOBACTERIUM TUBERCULOSIS; SIGNAL OUTPUT; SIGNAL TRANSMISSION; SINGLE-POINT MUTATION; TRANS-MEMBRANE SIGNALING;

AMINO ACIDS; BIOCHEMISTRY; ESCHERICHIA COLI; PHOSPHATASES; TAR;

BACTERIOLOGY;

ADENYLATE CYCLASE; ASPARTIC ACID; LIGAND; SERINE; BACTERIAL PROTEIN; ESCHERICHIA COLI PROTEIN; HYBRID PROTEIN; MEMBRANE PROTEIN; METHYL ACCEPTING CHEMOTAXIS PROTEINS; METHYL-ACCEPTING CHEMOTAXIS PROTEINS; TAR PROTEIN, E COLI;

ARTHROSPIRA PLATENSIS; ARTICLE; CHIMERA; CONTROLLED STUDY; CYANOBACTERIUM; ENZYME ASSAY; ESCHERICHIA COLI; IN VITRO STUDY; IN VIVO STUDY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PLASMID; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SIGNAL TRANSDUCTION; AMINO ACID SEQUENCE; CELL MEMBRANE; CHEMISTRY; CHEMORECEPTOR; CYTOLOGY; DRUG ANTAGONISM; ENZYMOLOGY; METABOLISM; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT;

ARTHROSPIRA PLATENSIS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MYCOBACTERIUM TUBERCULOSIS;

ADENYLATE CYCLASE; AMINO ACID SEQUENCE; ASPARTIC ACID; BACTERIAL PROTEINS; CELL MEMBRANE; CHEMORECEPTOR CELLS; CYANOBACTERIA; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; MYCOBACTERIUM TUBERCULOSIS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SERINE; SIGNAL TRANSDUCTION;

EID: 76249125189     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.051698     Document Type: Article

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