The role of the S1 domain in exoribonucleolytic activity: substrate specificity and multimerization.

@article{Amblar2007TheRO,
  title={The role of the S1 domain in exoribonucleolytic activity: substrate specificity and multimerization.},
  author={M{\'o}nica Amblar and Ana Barbas and Paulino G{\'o}mez-Puertas and Cec{\'i}lia M Arraiano},
  journal={RNA},
  year={2007},
  volume={13 3},
  pages={317-27}
}
RNase II is a 3'-5' exoribonuclease that processively hydrolyzes single-stranded RNA generating 5' mononucleotides. This enzyme contains a catalytic core that is surrounded by three RNA-binding domains. At its C terminus, there is a typical S1 domain that has been shown to be critical for RNA binding. The S1 domain is also present in the other major 3'-5' exoribonucleases from Escherichia coli: RNase R and polynucleotide phosphorylase (PNPase). In this report, we examined the involvement of the… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 21 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 58 references

Mutational analysis of polynucleotide phosphorylase from Escherichia coli

  • Jarrige, A.-C., D. Brechemier-Baey, N. Mathy, O. Duche, C. Portier
  • J. Mol. Biol. 321: 397.
  • 2002
Highly Influential
4 Excerpts

Recombinant PCR

  • R. Higuchi
  • PCR protocols. A guide to methods and…
  • 1990
Highly Influential
6 Excerpts

Similar Papers

Loading similar papers…