Mutations in residues involved in zinc binding in the catalytic site of Escherichia coli threonyl-tRNA synthetase confer a dominant lethal phenotype

Journal of Bacteriology

Volumn 189, Issue 19, 2007, Pages 6839-6848

  Caillet, Joël ^a   Graffe, Monique ^a   Eyermann, Flore ^b   Romby, Pascale ^b   Springer, Mathias ^a  

^a CNRS   (France)

^b INST DE BIOL MOLEC ET CELLULAIRE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

HETERODIMER; THREONINE TRANSFER RNA LIGASE;

AMINOACYLATION; ARTICLE; BACTERIAL GROWTH; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME SYNTHESIS; ESCHERICHIA COLI; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL;

CATALYTIC DOMAIN; DIMERIZATION; ESCHERICHIA COLI; GENE EXPRESSION REGULATION, BACTERIAL; MUTATION; PLASMIDS; PROTEIN BINDING; RNA, MESSENGER; THREONINE-TRNA LIGASE; ZINC;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 34948876353     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00439-07     Document Type: Article

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