Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 3'-half-tRNA molecule with a 5'-oH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end = a mature tRNA molecule containing a 2'-5'-phosphodiester bond
Substrates: the apparent requirement of Escherichia coli 2'-5' ligase for nucleoside modifications and the preference shown by this enzyme for a subset of Saccharomyces cerevisiae tRNA splicing substrates suggest that the Escherichia coli ligase is likely to act upon a tRNA or tRNA-like molecule in vivo. The tight binding of the RNA ligase to immobilized prokaryotic and eukaryotic tRNA provides evidence that the ligase recognizes a tRNA or tRNA-like substrate in vivo Products: -
?
3'-half-tRNA molecule with a 5'-OH end + 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end
mature tRNA molecule containing a 2'-5'-phosphodiester bond
Substrates: the reaction occurs possible through a one-step reaction involving hydrolysis of the 2',3'-cyclic phosphodiester bond and the simultaneous formation of a 2'-5'-phosphodiester bond. The reaction proceeds without added ATP or NAD+. The enzyme from Escherichia coli specifically ligates tRNA half-molecules (from Saccharomyces cerevisiae) containing nucleoside base modifications forming a 2'-5' phosphodiester bond at the ligated junction and shows a preference among different tRNA species, reversible in vitro. Yeast extract-modified pre-tRNATyr are the most active substrates tested for ligation by the Escherichia coli RNA ligase. tRNAPhe half-molecules produced by digestion of T7-transcribed pre-tRNAPhe with Saccharomyces cerevisiae tRNA splicing endonuclease are poorly ligated in Escherichia coli extracts Products: -
r
3'-half-tRNA molecule with a 5'-OH end + 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end
mature tRNA molecule containing a 2'-5'-phosphodiester bond
Substrates: the reaction occurs possible through a one-step reaction involving hydrolysis of the 2',3'-cyclic phosphodiester bond and the simultaneous formation of a 2'-5'-phosphodiester bond. The reaction proceeds without added ATP or NAD+ Products: -
Substrates: the apparent requirement of Escherichia coli 2'-5' ligase for nucleoside modifications and the preference shown by this enzyme for a subset of Saccharomyces cerevisiae tRNA splicing substrates suggest that the Escherichia coli ligase is likely to act upon a tRNA or tRNA-like molecule in vivo. The tight binding of the RNA ligase to immobilized prokaryotic and eukaryotic tRNA provides evidence that the ligase recognizes a tRNA or tRNA-like substrate in vivo Products: -
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli. Moderate overexpression of the ligase protein lead to slower growth rates and a temperature-sensitive phenotype in both wild-type and RNA ligase knockout strains
show
top
