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Protein component of Bacillus subtilis RNase P specifically enhances the affinity for precursor-tRNAAsp
J C Kurz1, S Niranjanakumari, C A Fierke
1Department of Biochemistry, Box 3711, Duke University Medical Center, Durham, North Carolina 27710, USA.
Biochemistry
|March 28, 1998
Abstract:
Ribonuclease P (RNase P) is an endonuclease that cleaves precursor tRNA to form the 5'-end of mature tRNA and is composed of a catalytic RNA subunit and a small protein subunit. The function of the protein component of Bacillus subtilis RNase P in catalysis of B. subtilis precursor tRNAAsp cleavage has been elucidated using steady-state kinetics, transient kinetics, and ligand affinity measurements to compare the functional properties of RNase P holoenzyme to RNase P RNA in 10 mM MgCl2, 100 mM NH4Cl. The protein component modestly affects several steps including