Mechanism of action of a yeast RNA ligase in tRNA splicing

@article{Greer1983MechanismOA,
  title={Mechanism of action of a yeast RNA ligase in tRNA splicing},
  author={Chris L. Greer and Craig L. Peebles and Peter A Gegenheimer and John Abelson},
  journal={Cell},
  year={1983},
  volume={32},
  pages={537-546}
}
Purification of yeast transfer RNA ligase.
Conserved mechanism of tRNA splicing in eukaryotes
TLDR
It is demonstrated in this study the existence of a yeast tRNA ligase-like activity in HeLa cells, and the entire yeastlike tRNA splicing machinery is intact, arguing that the mechanism of t RNA splicing is conserved among eukaryotes.
Transient ADP-ribosylation of a 2′-Phosphate Implicated in Its Removal from Ligated tRNA during Splicing in Yeast*
TLDR
It is shown here that KptA protein removes the 2′-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated followed by a presumed transesterification to release the RNA and generate Appr>p.
Domain structure in yeast tRNA ligase.
TLDR
Evidence is provided for a model in which the three constituent activities of ligase are located in three distinct domains separated by protease-sensitive regions, and the active adenylylated site in the ligase domains is lysine-114.
The 2′-5′ RNA Ligase of Escherichia coli
TLDR
The RNA ligase reaction was studied in vitro using purified enzyme and was found to be reversible, indicating that this enzyme may perform cleavage or ligation in vivo.
A highly specific phosphatase from Saccharomyces cerevisiae implicated in tRNA splicing
TLDR
It is suggested that this phosphatase identified and partially purified from crude extracts of Saccharomyces cerevisiae cells is responsible for the completion of tRNA splicing in vivo, based primarily on its specificity for the 2'-phosphate of spliced tRNA and on the resistance of the splice junction 2'- phosphate to a nonspecific phosphat enzyme.
Genetic and Biochemical Analysis of the Functional Domains of Yeast tRNA Ligase*
TLDR
The results suggest that GTP is the physiological substrate and that the Trl1 kinase has a single NTP binding site of which the P-loop is a component.
Use of domain enzymes from wheat RNA ligase for in vitro preparation of RNA molecules.
Characterization of the Adenylation Site in the RNA 3′-Terminal Phosphate Cyclase from Escherichia coli *
TLDR
This work assigns the site of adenylation in the E. coli cyclase to His-309, a histidine residue that is conserved in all members of the class I subfamily of cyclases identified by phylogenetic analysis.
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