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Partial Purification and Characterization of Enzymes Involved in the Processing of Pre-M1 RNA at the 3' End in Escherichia coli
Partial Purification and Characterization of Enzymes Involved in the Processing of Pre-M1 RNA at the 3' End in Escherichia coli
Journal of the Korean Chemical Society. 1999. Jun, 43(3): 307-314
  • Published : June 00, 1999
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Kim, Ha Dong
Ko, Jae Hyeong
Cho, Bong Rae
Lee, Young Hoon
Park, In Won

Abstract
Ml RNA, the RNA component of RNase P from Escherichia coli, is produced by 3' processing of pre-Ml RNA, a major primary transcript of the rnpB gene. The enzyme fraction containing the processing activity was partially purified and characterized. Since exposure of the active fraction to the high salt condition results in the inactivation of the processing activity, the processing enzyme seems to be an enzyme complex composed of multiple enzymes. The enzyme fraction loses the processing activity when treated with the chemical nuclease lead(II) ion, but regains its activity by the addition of RNA isolated from the enzyme fraction itself, suggesting that an RNA molecule(s) may be essential for the processing activity. Analysis of cleavage sites produced by the partially purified enzyme fraction also implies that the 3' processing occurs by multiple enzymes and at least in two distinct pathways.