A base pair at the bottom of the anticodon stem is reciprocally preferred for discrimination of cognate tRNAs by Escherichia coli lysyl- and glutaminyl-tRNA synthetases

Nucleic Acids Research

Volumn 34, Issue 10, 2006, Pages 3181-3188

  Fukunaga, Jun Ichi ^a   Ohno, Satoshi ^a   Nishikawa, Kazuya ^a   Yokogawa, Takashi ^a  

^a GIFU UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; BETA GALACTOSIDASE; GLUTAMINE TRANSFER RNA LIGASE; LYSINE TRANSFER RNA LIGASE; TRANSFER RNA; TYROSINE TRANSFER RNA LIGASE; GLUTAMINE; GLUTAMINYL-TRNA SYNTHETASE; LYSINE; LYSINE TRANSFER RNA; TYROSINE TRANSFER RNA;

AMINO ACID SUBSTITUTION; AMINOACYLATION; ANIMAL CELL; ANTICODON; ARTICLE; BASE PAIRING; CONTROLLED STUDY; ENZYME ACTIVITY; ESCHERICHIA COLI; GENETIC ENGINEERING; MOLECULAR RECOGNITION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN SYNTHESIS; RNA STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; ENZYMOLOGY; GENE REPRESSION; GENETICS; METABOLISM; MOLECULAR GENETICS;

ESCHERICHIA COLI;

AMINO ACYL-TRNA SYNTHETASES; ANTICODON; BASE PAIRING; BASE SEQUENCE; ESCHERICHIA COLI; GLUTAMINE; LYSINE; LYSINE-TRNA LIGASE; MOLECULAR SEQUENCE DATA; RNA, TRANSFER, LYS; RNA, TRANSFER, TYR; SUBSTRATE SPECIFICITY; SUPPRESSION, GENETIC; TRANSFER RNA AMINOACYLATION;

EID: 33745365951     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkl414     Document Type: Article

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