Abstract
Ribonuclease P: function and variation.
Highlights
Most information regarding RNase P derives from work with Escherichia coli and Bacillus subtilis, representatives of two of the dozen major eubacterial phyla defined by rRNA sequence comparisons [4]
The RNase P holoenzyme and RNA-alone activities of B. subtilis and E. coli are similar in their salt selectivity and response to ionic strength [5, 6]
The common result from kinetic studies is that substrates lacking the sequence CCA are acted upon by the holoenzyme or the RNase P RNA with a K, about lo-fold higher than substrates containing CCA
Summary
Makes no substantial specific contacts with the substrate during the RNase P reaction. The common result from kinetic studies is that substrates lacking the sequence CCA are acted upon by the holoenzyme or the RNase P RNA with a K,,, about lo-fold higher than substrates containing CCA. This indicates an interaction between RNase P and the CCA terminus of the mature tRNA that contributes about 5 kJ/mol of binding energy to the enzyme-substrate complex,’ about the contribution expected for a single hydrogen bond in an aqueous solvent [28]. The common theme among the nuclear RNase P from HeLa cells or the yeasts is that the enzymes are large (about I5 S by sedimentation) and they are inactivated by treatment with micrococcal nuclease, indicating the presence
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