Structure in solution of M1 RNA, the catalytic subunit of ribonuclease P from Escherichia coli.
The structure of M1 RNA, the RNA component of Escherichia coli RNase P, has been probed by mild digestion with a variety of ribonucleases. The results have been used to generate a model for the two-dimensional structure of M1 RNA. This model is similar in many respects to an earlier model that was based entirely on theoretical considerations. M1 RNA was digested with RNase T1 in buffer containing 10 mM MgCl2 (in which M1 RNA, by itself, has no catalytic activity) and in buffer containing 60 mM MgCl2 (in which M1 RNA can cleave precursors to tRNA molecules). Under these conditions, the main features of the secondary structure are similar, but several minor differences are apparent. Such subtle changes in structure are also observed when M1 RNA is present in a binary complex with a substrate molecule, the precursor to E. coli tRNATyr.
D004722:Endoribonucleases / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D012329:RNA, Bacterial / Q000378:metabolism; D043262:Ribonuclease P
D029968:Escherichia coli Proteins; D012329:RNA, Bacterial; D004722:Endoribonucleases; D043262:Ribonuclease P; C470865:ribonuclease P, E coli