Bacterial RNase P: a new view of an ancient enzyme
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Immunology and Microbiology,Microbiology,Infectious Diseases
Link
http://www.nature.com/articles/nrmicro1491.pdf
Reference132 articles.
1. Frank, D. N. & Pace, N. R. Ribonuclease P: unity and diversity in a tRNA processing ribozyme. Annu. Rev. Biochem. 67, 153–180 (1998).
2. Walker, S. C. & Engelke, D. R. Ribonuclease P: the evolution of an ancient RNA enzyme. Crit. Rev. Biochem. Mol. Biol. 41, 77–102 (2006).
3. Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N. & Altman, S. The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell 35, 849–857 (1983). Reports the discovery that the RNA of bacterial RNase P is catalytically proficient in the absence of the protein moiety of the enzyme.
4. Pannucci, J. A., Haas, E. S., Hall, T. A., Harris, J. K. & Brown, J. W. RNase P RNAs from some archaea are catalytically active. Proc. Natl Acad. Sci. USA 96, 7803–7808 (1999).
5. Schedl, P. & Primakoff, P. Mutants of Escherichia coli thermosensitive for the synthesis of transfer RNA. Proc. Natl Acad. Sci. USA 70, 2091–2095 (1973).
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