The aspartate chemoreceptor Tar is effectively methylated by binding to the methyltransferase mainly through hydrophobic interaction

Molecular Microbiology

Volumn 36, Issue 1, 2000, Pages 132-140

  Shiomi, Daisuke ^a   Okumura, Hisashi ^a,b   Homma, Michio ^a   Kawagishi, Ikuro ^a  

^a NAGOYA UNIVERSITY   (Japan)

^b Nichirei Corporation   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; ASPARTIC ACID; HYBRID PROTEIN; METHYLTRANSFERASE;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMORECEPTOR; CHEMOTAXIS; CRYSTAL STRUCTURE; DEMETHYLATION; ESCHERICHIA COLI; GENE EXPRESSION; HYDROGEN BOND; HYDROPHOBICITY; METHYLATION; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

ASPARTIC ACID; BACTERIAL PROTEINS; BINDING SITES; CHEMORECEPTORS; CHEMOTAXIS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MEMBRANE PROTEINS; METHYLATION; METHYLTRANSFERASES; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; RECEPTORS, CELL SURFACE;

ESCHERICHIA COLI;

EID: 0034079029     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2000.01834.x     Document Type: Article

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