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In vitro transactivation of Bacillus subtilis RNase P RNA
Author(s) -
Kim Hadong,
Poelling Richard R,
Leeper Thomas C,
Meyer Melissa A,
Schmidt Francis J
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02929-5
Subject(s) - ribozyme , transactivation , rnase p , enzyme kinetics , rna , vs ribozyme , chemistry , bacillus subtilis , microbiology and biotechnology , biology , stereochemistry , catalysis , biochemistry , active site , genetics , gene , gene expression , bacteria
Deletion of the ‘signature’ PL5.1 stem‐loop structure of a Type II RNase P RNA diminished its catalytic activity. Addition of PL5.1 in trans increased catalytic efficiency ( k cat / K M ) rather than k cat . Transactivation was due to the binding of a single PL5.1 species per ribozyme with an apparent K d near 600 nM. The results are consistent with the role of PL5.1 being to position the substrate near the active site of the ribozyme, and with the hypothesis that ribozymes can evolve by accretion of preformed smaller structures.