In vitro transactivation of Bacillus subtilis RNase P RNA.
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 (kcat/KM) rather than kcat. Transactivation was due to the binding of a single PL5.1 species per ribozyme with an apparent Kd 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.
Kim
H
H
Department of Biochemistry, M121 Medical Sciences, University of Missouri-Columbia, 65212, USA.
Poelling
R R
RR
Leeper
T C
TC
Meyer
M A
MA
Schmidt
F J
FJ
D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D001483:Base Sequence; D002384:Catalysis; D004722:Endoribonucleases / Q000235:genetics* / Q000378:metabolism; D019143:Evolution, Molecular; D007700:Kinetics; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D012329:RNA, Bacterial / Q000737:chemistry / Q000235:genetics*; D016337:RNA, Catalytic / Q000235:genetics* / Q000378:metabolism; D043262:Ribonuclease P; D013379:Substrate Specificity; D015533:Transcriptional Activation
D012329:RNA, Bacterial; D016337:RNA, Catalytic; D004722:Endoribonucleases; D043262:Ribonuclease P