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Protein activation of a ribozyme the role of bacterial RNase P protein
Protein activation of a ribozyme: the role of bacterial RNase P protein.
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Bacterial ribonuclease P (RNase P) belongs to a class of enzymes that utilize both RNAs and proteins to perform essential cellular functions. The bacterial RNase P protein is required to activate bacterial RNase P RNA in vivo, but previous studies have yielded contradictory conclusions regarding its specific functions. Here, we use biochemical and biophysical techniques to examine all of the proposed functions of the protein in both Escherichia coli and Bacillus subtilis RNase P. We demonstrate that the E. coli protein, but not the B. subtilis protein, stabilizes the global structure of RNase P RNA, although both proteins influence holoenzyme dimer formation and precursor tRNA recognition to different extents. By comparing each protein in complex with its cognate and noncognate RNA, we show that differences between the two types of holoenzymes reside primarily in the RNA and not the protein components of each. Our results reconcile previous contradictory conclusions regarding the role of the protein and support a model where the protein activates local RNA structures that manifest multiple holoenzyme properties.
Buck AH, Dalby AB, Poole AW, Kazantsev AV, Pace NR
The EMBO journal
2005-10-05 00:00
24
19
3360-8
Bacillus subtilis,Electrophoresis,Electrophoretic Mobility Shift Assay,Enzyme Activation,Escherichia coli,Holoenzymes,Models, Biological,RNA, Catalytic,RNA, Transfer,Ribonuclease P,Species Specificity,Holoenzymes,RNA, Catalytic,RNA, Transfer,Ribonuclease P
Department of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO 80309, USA
EMBO J.
NIGMS GM-34527, NIGMS T32 GM-65103
0261-4189
10.1038/sj.emboj.7600805
7600805
966
True
16163391
