Evidence that 16S RNA from E. coli can assume two different biologically active conformations.
We have recently shown that 16S RNA can be extracted from 30S ribosomes by an acetic acid-urea precipitation procedure which yields RNA capable of binding 13 individual ribosomal proteins. This is in contrast to phenol extracted 16S RNA which can specifically associate with only 7 proteins2-7. In the experiments reported here, we demonstrate that the difference in protein binding capacities is due to a relatiely more "open" configuration possessed by the acetic acid-urea 16S RNA. Under identical conditions, acetic acid-urea 16S RNA is more susceptible to limited T1-RNase digestion than is phenol-16S RNA. In addition, acetic acid-urea RNA shows a relatively slower electrophoretic mobility. The observable difference in conformation between the two types of RNA is lost by storage at-70 degrees C. This loss is accompanied by a reduction in protein binding capacity of the acetic acid-urea 16S RNA.
D001483:Base Sequence; D001665:Binding Sites; D002499:Centrifugation, Density Gradient; D004355:Drug Stability; D004587:Electrophoresis, Agar Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism*; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D009690:Nucleic Acid Conformation; D010636:Phenols; D011485:Protein Binding; D012335:RNA, Ribosomal / Q000378:metabolism; D012260:Ribonucleases / Q000378:metabolism; D012269:Ribosomal Proteins / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism; D014508:Urea
D046911:Macromolecular Substances; D010636:Phenols; D012335:RNA, Ribosomal; D012269:Ribosomal Proteins; D014508:Urea; D012260:Ribonucleases