Type A and B RNase P RNAs are interchangeable in vivo despite substantial biophysical differences.
We show that structural type A and B bacterial ribonuclease P (RNase P) RNAs can fully replace each other in vivo despite the many reported differences in their biogenesis, biochemical/biophysical properties and enzyme function in vitro. Our findings suggest that many of the reported idiosyncrasies of type A and B enzymes either do not reflect the in vivo situation or are not crucial for RNase P function in vivo, at least under standard growth conditions. The discrimination of mature tRNA by RNase P, so far thought to prevent product inhibition of the enzyme in the presence of a large cellular excess of mature tRNA relative to the precursor form, is apparently not crucial for RNase P function in vivo.
Institut für Pharmazeutische Chemie, Philipps-Universität Marburg, Germany.
Barbara
B
Wegscheid
Ciarán
C
Condon
Roland K
RK
Hartmann
D001412:Bacillus subtilis / Q000166:cytology / Q000201:enzymology / Q000235:genetics; D001483:Base Sequence; D049109:Cell Proliferation; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D020035:Holoenzymes / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D009690:Nucleic Acid Conformation; D012329:RNA, Bacterial / Q000737:chemistry / Q000145:classification* / Q000235:genetics* / Q000378:metabolism; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D043262:Ribonuclease P / Q000737:chemistry* / Q000235:genetics*; D014158:Transcription, Genetic / Q000235:genetics
D020035:Holoenzymes; D012329:RNA, Bacterial; D011994:Recombinant Proteins; D043262:Ribonuclease P