The P3 domain of E. coli ribonuclease P RNA can be truncated and replaced.
We prepared some truncated and replaced P3 mutants of Escherichia coli RNase P RNA, and used them to examine the RNase P ribozyme and holoenzyme reactions of a pre-tRNA substrate. The results indicated that mutations in the P3 domain did not affect the cleavage site selection of the pre-tRNA substrate, but did affect the efficiency of cleavage of the substrate. Results of stepwise truncation of the P3 domain and its replacement by the TAR sequence showed that the P3 domain of the E. coli RNase P was able to be truncated to certain length and was replaceable, but could not be deleted in the ribozyme.
Tanaka
Terumichi
T
Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempakucho, Toyohashi, Aichi 441-8580, Japan. tanakat@eco.tut.ac.jp
Kanda
Naomi
N
Kikuchi
Yo
Y
D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010802:Phylogeny; D012329:RNA, Bacterial / Q000737:chemistry*; D043262:Ribonuclease P / Q000235:genetics*
D012329:RNA, Bacterial; D043262:Ribonuclease P