© 2004 by Oxford University Press
Mutational analyses of neighboring domains of active center of RNase P ribozyme
Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempakucho, Toyohashi, Aichi 441-8580, Japan
We prepared series of P2
P4 domain variants of Escherichia coli ribonuclease P (RNase P) ribozyme, and examined enzymatic activities of them. The results indicated that mutations in these domains did not affect the cleavage site selection of the enzyme, but affected cleavage efficiencies and dependence on magnesium ion concentrations.