Plant tRNA ligases are multifunctional enzymes that have diverged in sequence and substrate specificity from RNA ligases of other phylogenetic origins

Nucleic Acids Research

Volumn 33, Issue 1, 2005, Pages 388-399

  Englert, Markus ^a   Beier, Hildburg ^a  

^a UNIVERSITY OF WÜRZBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE PHOSPHATE; PHOSPHODIESTERASE; POLYNUCLEOTIDE 5' HYDROXYL KINASE; RNA LIGASE; TRANSFER RNA; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARABIDOPSIS; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; COLUMN CHROMATOGRAPHY; CONTROLLED STUDY; COVALENT BOND; ENZYME ACTIVITY; ENZYME SPECIFICITY; EUKARYOTE; GENETIC CONSERVATION; GENETIC VARIABILITY; IN VITRO STUDY; IN VIVO STUDY; INTRON; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYLOGENY; PLANT GENETICS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DATABASE; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PURIFICATION; RICE; RNA PROCESSING; RNA PURIFICATION; RNA SEQUENCE; RNA SPLICING; SEQUENCE HOMOLOGY; WHEAT GERM; CLASSIFICATION; ENZYMOLOGY; GENE; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; PLANT; SACCHAROMYCES CEREVISIAE; WHEAT;

AMINO ACID SEQUENCE; ARABIDOPSIS; GENES, PLANT; MOLECULAR SEQUENCE DATA; PHYLOGENY; PLANTS; RECOMBINANT PROTEINS; RNA LIGASE (ATP); RNA SPLICING; RNA, TRANSFER; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TRITICUM;

EID: 13744262410     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gki174     Document Type: Article

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