PMID:1717693

Citation	Peck-Miller, KA and Altman, S (1991) Kinetics of the processing of the precursor to 4.5 S RNA, a naturally occurring substrate for RNase P from Escherichia coli. J. Mol. Biol. 221:1-5
Abstract	A study was made of the cleavage by M1 RNA and RNase P of a non-tRNA precursor that can serve as a substrate for RNase P from Escherichia coli, namely, the precursor to 4.5 S RNA (p4.5S). The overall efficiency of cleavage of p4.5S by RNase P is similar to that of wild-type tRNA precursors. However, unlike the reaction with wild-type tRNA precursors, the reaction catalyzed by the holoenzyme with p4.5S as substrate has a much lower Km value than that catalyzed by M1 RNA with the same substrate, indicating that the protein subunit plays a crucial role in the recognition of p4.5S. A model hairpin substrate, based on the sequence of p4.5S, is cleaved with greater efficiency than the parent molecule. The 3'-terminal CCC sequence of p4.5 S may be as important for cleavage of this substrate as the 3'-terminal CCA sequence is for cleavage of tRNA precursors.
Links	PubMed
Keywords	Base Sequence; Endoribonucleases/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Kinetics; Molecular Sequence Data; Nucleic Acid Conformation; RNA Precursors/metabolism; RNA Processing, Post-Transcriptional; RNA, Bacterial/metabolism; RNA, Catalytic/metabolism; Ribonuclease P; Substrate Specificity
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