Cleavage efficiences of model substrates for ribonuclease P from Escherichia coli and Thermus thermophilus

We compared cleavage efficiencies of mono-molecular and bipartite model RNAs as substrates for RNase P RNAs (M1 RNAs) and holoenzymes from E. coli and Thermus thermophilus , an extreme thermophilic eubacterium. Acceptor stem and T arm of pre-tRNA substrates are essential recognition elements for bot...

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Bibliographic Details
Published in:Nucleic acids research 1992, Vol.20 (22), p.5963-5970
Main Authors: SCHLEGL, J, FÜRSTE, J. P, BALD, R, ERDMANN, V. A, HARTMANN, R. K
Format: Article
Language:English
Subjects:
Bacteriology
Biological and medical sciences
Escherichia coli
Fundamental and applied biological sciences. Psychology
Metabolism. Enzymes
Microbiology
Thermus thermophilus
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Summary:We compared cleavage efficiencies of mono-molecular and bipartite model RNAs as substrates for RNase P RNAs (M1 RNAs) and holoenzymes from E. coli and Thermus thermophilus , an extreme thermophilic eubacterium. Acceptor stem and T arm of pre-tRNA substrates are essential recognition elements for both enzymes. Impairing coaxial stacking of acceptor and T stems and omitting the T loop led to reduced cleavage efficiencies. Small model substrates were less efficiently cleaved by M1 RNA and RNase P from T. thermophilus than by the corresponding E. coli activities. Competition kinetics and gel retardation studies showed that truncated tRNA substrates are less tightly bound by RNase P and M1 RNA from both bacteria.
ISSN:0305-1048
1362-4962