Mutational analyses of neighboring domains of active center of RNase P ribozyme.
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.
Tanaka
Terumichi
T
Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempakucho, Toyohashi, Aichi 441-8580, Japan.
Haga
Shinnosuke
S
Kanda
Naomi
N
Ando
Tomoaki
T
Kikuchi
Yo
Y
D001483:Base Sequence; D001665:Binding Sites; D004252:DNA Mutational Analysis; D004926:Escherichia coli / Q000201:enzymology*; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D043262:Ribonuclease P / Q000737:chemistry* / Q000235:genetics*; D013329:Structure-Activity Relationship
D043262:Ribonuclease P