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}
}
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217 Citations
Highly Influential Citations
4
Background Citations
57
Methods Citations
8
Results Citations
2

217 Citations

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.
Highly purified transfer RNA splicing endonuclease from Saccharomyces cerevisiae.
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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References

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Splicing of yeast tRNA precursors: structure of the reaction intermediates
Origin of splice junction phosphate in tRNAs processed by HeLa cell extract
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TLDR
It is suggested that an enzyme-AMP intermediate occurs during the course of the RNA ligase reaction, which requires ATP and leads to the formation of AMP and PPi.
Splicing of yeast tRNA precursors: a two-stage reaction
Bacteriophage T4 RNA ligase. Reaction intermediates and interaction of substrates.
Nuclear ligation of RNA 5'-OH kinase products in tRNA
TLDR
The results presented suggest splicing of several mouse L-cell tRNA species in isolated nuclei which involve the RNA 5'-OH kinase products as intermediates and gamma-32P from ATP in vitro predominantly in 5'-monophosphoryl termini and internal phosphodiester bonds with a nonrandom nearest-neighbor distribution.
Yeast tRNA3Leu gene transcribed and spliced in a HeLa cell extract.
TLDR
The results stress the extraordinary conservation of tRNA biosynthesis in eukaryotes and demonstrate that a HeLa extract provides a useful system for investigating this process.
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TLDR
A precursor of yeast tRNATyr is isolated and shown that it contains an intervening sequence identical to that found in the gene for tR NATyr, which is functionally inactive as it cannot be aminoacylated and the anticodon is not accessible for hydrogen bonding.
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Bacteriophage T4 RNA ligase: preparation of a physically homogeneous, nuclease-free enzyme from hyperproducing infected cells.
TLDR
It was discovered that adenylalation of the enzyme--a step in the reaction pathway--markedly decreased the electrophoretic mobility of RNA ligase through polyacrylamide gels containing sodium dodecyl sulfate, which allows identification ofRNA ligase among a mixture of proteins and was used to demonstrate that virtually all of the purified protein is enzymatically active.
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