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Lead-ion-induced cleavage of RNase P RNA
- Source :
- European Journal of Biochemistry. 219:49-56
- Publication Year :
- 1994
- Publisher :
- Wiley, 1994.
-
Abstract
- Pb(2+)-induced hydrolysis of RNase P RNAs from Escherichia coli and the thermophilic eubacterium Thermus thermophilus HB8 revealed one prominent site-specific cleavage in the two RNAs and several minor cleavage sites in structurally corresponding regions of both RNAs. Data presented here and in a previous study [Kazakov, S.Altman, S. (1991) Proc. Natl Acad. Sci. USA 88, 9193-9197] provide evidence for several ubiquitous metal-ion-binding sites in eubacterial RNase P RNA subunits. With the T. thermophilus RNase P RNA, susceptibility to Pb(2+)-induced strand scission at the most prominent site was hypersensitive at the temperature of highest enzyme activity (55 degrees C). Pb2+ hydrolysis at this site was strongly reduced at a temperature of 37 degrees C, where processing is also inefficient. For E. coli RNase P RNA, specific changes in the lead hydrolysis pattern were observed due to the presence of excess tRNA. Thus, Pb(2+)-induced hydrolysis seems suitable to sense different conformations of RNase P RNAs. The T. thermophilus RNase P RNA, in particular, displayed significant processing activity after severe fragmentation by Pb2+, and therefore appears to be suited for reconstituting an active enzyme from RNA subfragments.
- Subjects :
- Transcription, Genetic
RNase P
Molecular Sequence Data
Biochemistry
RNase PH
Ribonuclease P
Endoribonucleases
Escherichia coli
RNA, Catalytic
RNase H
Binding Sites
Base Sequence
biology
Escherichia coli Proteins
Hydrolysis
Thermus thermophilus
RNA
Non-coding RNA
biology.organism_classification
Molecular biology
Kinetics
RNase MRP
Lead
Transfer RNA
biology.protein
Nucleic Acid Conformation
Thermodynamics
Subjects
Details
- ISSN :
- 14321033 and 00142956
- Volume :
- 219
- Database :
- OpenAIRE
- Journal :
- European Journal of Biochemistry
- Accession number :
- edsair.doi.dedup.....d85d2493a88f4b77c6cec4768e24229c