3'-end processing of precursor M1 RNA by the N-terminal half of RNase E.
M1 RNA, the catalytic component of Escherichia coli RNase P, is derived from the 3'-end processing of precursor M1 RNA, a major transcript of the rnpB gene. In this study, we investigated the mechanism of 3'-end processing of M1 RNA using the recombinant N-terminal half RNase E. The cleavage site preference of RNase E differed from that of the 40% ammonium sulfate precipitate (ASP-40), a partially purified cell extract containing processing activity. However, the addition of a trace amount of ASP-40 changed the cleavage site preference of RNase E to that of ASP-40 suggesting the involvement of a soluble factor in cleavage site preference.
Sim
Soyeong
S
Department of Chemistry, Center for Molecular Design and Synthesis, Korea Advanced Institute of Science and Technology, Taejon 305-701, South Korea.
Kim
Kwang-sun
KS
Lee
Younghoon
Y
D001483:Base Sequence; D002850:Chromatography, Gel; D017931:DNA Primers; D004722:Endoribonucleases / Q000378:metabolism*; D009690:Nucleic Acid Conformation; D012313:RNA / Q000737:chemistry / Q000378:metabolism*; D012322:RNA Precursors / Q000737:chemistry / Q000378:metabolism*; D012323:RNA Processing, Post-Transcriptional
D017931:DNA Primers; D012322:RNA Precursors; D012313:RNA; D004722:Endoribonucleases; C022537:ribonuclease E