Escherichia coli tRNAs are resistant to the hyperprocessing reaction of homologous E. coli ribonuclease P ribozyme.
Bacterial ribonuclease P RNA ribozyme can do the hyperprocessing reaction, the internal cleavage reaction of some floppy eukaryotic tRNAs. The hyperprocessing reaction can be used as a detection tool to examine the stability of the cloverleaf shape of tRNA. Until now, the hyperprocessing reaction has been observed in the heterologous combination of eukaryotic tRNAs and bacterial RNase P enzymes. In this paper, we examined the hyperprocessing reaction of Escherichia coli tRNAs by homologous E. coli RNase P, to find that these homologous tRNAs were resistant to the toxic hyperprocessing reaction. Our results display the evidence for molecular co-evolution between homologous tRNAs and RNase P in the bacterium E. coli.
Tanaka
Terumichi
T
Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku-cho, Toyohashi, Aichi 441-8580, Japan. tanakat@eco.tut.ac.jp
Ando
Tomoaki
T
Sakai
Etsuko
E
Hahisba
Taka-aki
TA
Hori
Yoshiaki
Y
Kikuchi
Yo
Y
D001412:Bacillus subtilis / Q000737:chemistry; D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D012329:RNA, Bacterial / Q000737:chemistry*; D012343:RNA, Transfer / Q000737:chemistry*; D043262:Ribonuclease P / Q000737:chemistry*
D012329:RNA, Bacterial; D012343:RNA, Transfer; D043262:Ribonuclease P