Engineering Giardia lamblia trimethylguanosine synthase (GlaTgs2) to transfer non-natural modifications to the RNA 5'-cap.

@article{Holstein2015EngineeringGL,
  title={Engineering Giardia lamblia trimethylguanosine synthase (GlaTgs2) to transfer non-natural modifications to the RNA 5'-cap.},
  author={J. M. Holstein and D. Stummer and A. Rentmeister},
  journal={Protein engineering, design \& selection : PEDS},
  year={2015},
  volume={28 6},
  pages={
          179-86
        }
}
Trimethylguanosine synthase from Giardia lamblia (GlaTgs2) naturally catalyzes methyl transfer from S-adenosyl-L-methionine (AdoMet) to the exocyclic N(2) atom of the 5'-cap--a hallmark of eukaryotic mRNAs. The wild-type enzyme shows substrate promiscuity and can also use the AdoMet-analog AdoPropen for allyl transfer. Here we report on engineering GlaTgs2 to enhance the activity on AdoPropen. A mutational analysis, involving an alanine scan of 10 residues located around the active site, was… Expand
Chemo-enzymatic modification of eukaryotic mRNA.
...
1
2
3
...

References

SHOWING 1-10 OF 73 REFERENCES
Giardia lamblia RNA Cap Guanine-N2 Methyltransferase (Tgs2)*
Structure analysis of the conserved methyltransferase domain of human trimethylguanosine synthase TGS1.
Yeast-like mRNA Capping Apparatus in Giardia lamblia*
Encephalitozoon cuniculi mRNA Cap (Guanine N-7) Methyltransferase
Characterization of a mimivirus RNA cap guanine-N2 methyltransferase.
Genetic and Biochemical Analysis of Yeast and Human Cap Trimethylguanosine Synthase
Labeling substrates of protein arginine methyltransferase with engineered enzymes and matched S-adenosyl-L-methionine analogues.
...
1
2
3
4
5
...