NDLI: Alternative substrate kinetics of Escherichia coli ribonuclease P: determination of relative rate constants by internal competition.

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Alternative substrate kinetics of Escherichia coli ribonuclease P: determination of relative rate constants by internal competition.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Yandek, Lindsay E. Harris, Michael E. Lin, Hsuan-chun
Description	Author Affiliation: Yandek LE ( Department of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106, USA.)
Abstract	A single enzyme, ribonuclease P (RNase P), processes the 5' ends of tRNA precursors (ptRNA) in cells and organelles that carry out tRNA biosynthesis. This substrate population includes over 80 different competing ptRNAs in Escherichia coli. Although the reaction kinetics and molecular recognition of a few individual model substrates of bacterial RNase P have been well described, the competitive substrate kinetics of the enzyme are comparatively unexplored. To understand the factors that determine how different ptRNA substrates compete for processing by E. coli RNase P, we compared the steady state reaction kinetics of two ptRNAs that differ at sequences that are contacted by the enzyme. For both ptRNAs, substrate cleavage is fast relative to dissociation. As a consequence, V/K, the rate constant for the reaction at limiting substrate concentrations, reflects the substrate association step for both ptRNAs. Reactions containing two or more ptRNAs follow simple competitive alternative substrate kinetics in which the relative rates of processing are determined by ptRNA concentration and their V/K. The relative V/K values for eight different ptRNAs, which were selected to represent the range of structure variation at sites contacted by RNase P, were determined by internal competition in reactions in which all eight substrates were present simultaneously. The results reveal a relatively narrow range of V/K values, suggesting that rates of ptRNA processing by RNase P are tuned for uniform specificity and consequently optimal coupling to precursor biosynthesis.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	12
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-03-22
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Escherichia Coli Proteins Chemistry Escherichia Coli Enzymology Ribonuclease P Algorithms Binding, Competitive Kinetics Molecular Sequence Data Nucleic Acid Conformation Protein Binding RNA Cleavage RNA Processing, Post-Transcriptional RNA, Bacterial RNA, Transfer Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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