The osmotic activation of transporter ProP is tuned by both its C-terminal coiled-coil and osmotically induced changes in phospholipid composition

Journal of Biological Chemistry

Volumn 280, Issue 50, 2005, Pages 41387-41394

  Tsatskis, Yonit ^a,c   Khambati, Jumana ^a,d   Dobson, Martina ^a   Bogdanov, Mikhail ^b   Dowhan, William ^b   Wood, Janet M ^a  

^a UNIVERSITY OF GUELPH   (Canada)

^b UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

^c MOUNT SINAI HOSPITAL   (Canada)

^d UNIVERSITY OF CALGARY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BIOLOGICAL MEMBRANES; DERIVATIVES; MOLECULAR BIOLOGY; MOLECULAR STRUCTURE; PHOSPHOLIPIDS;

AGROBACTERIUM TUMEFACIENS (PROPAT); CORYNEBACTERIUM GLUTAMICUM (PROPCG); HELICAL COILED-COIL; OSMOTIC ACTIVATION;

ESCHERICHIA COLI;

ARGININE; CARDIOLIPIN; CARRIER PROTEIN; LIGAND; PHOSPHOLIPID; PROTEIN PROP; PROTEIN PROQ; UNCLASSIFIED DRUG;

ADAPTATION; ALPHA HELIX; ARTICLE; BACTERIAL GROWTH; CARBOXY TERMINAL SEQUENCE; CORYNEBACTERIUM GLUTAMICUM; CULTURE MEDIUM; ESCHERICHIA COLI; LIPID COMPOSITION; NONHUMAN; OSMOLALITY; OSMOREGULATION; OSMOSIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LIPID INTERACTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RHIZOBIUM RADIOBACTER;

AMINO ACID SEQUENCE; ARGININE; ASPARTIC ACID; BINDING SITES; BIOLOGICAL TRANSPORT; BLOTTING, WESTERN; CARDIOLIPINS; CELL MEMBRANE; CODON, TERMINATOR; CULTURE MEDIA; DOSE-RESPONSE RELATIONSHIP, DRUG; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE DELETION; IONS; LIGANDS; LIPIDS; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE TRANSPORT PROTEINS; MODELS, CHEMICAL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OSMOLAR CONCENTRATION; OSMOSIS; PHOSPHOLIPIDS; PLASMIDS; POTASSIUM; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, SCAVENGER; SYMPORTERS;

AGROBACTERIUM TUMEFACIENS; BACTERIA (MICROORGANISMS); CORYNEBACTERIUM GLUTAMICUM; ESCHERICHIA COLI;

EID: 29244463867     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M508362200     Document Type: Article

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