Long-range structure in ribonuclease P RNA.
Phylogenetic-comparative and mutational analyses were used to elucidate the structure of the catalytically active RNA component of eubacterial ribonuclease P (RNase P). In addition to the refinement and extension of known structural elements, the analyses revealed a long-range interaction that results in a second pseudoknot in the RNA. This feature strongly constrains the three-dimensional structure of RNase P RNA near the active site. Some RNase P RNAs lack this structure but contain a unique, possibly compensating, structural domain. This suggests that different RNA structures located at different positions in the sequence may have equivalent architectural functions in RNase P RNA.
Haas
E S
ES
Department of Biology, Indiana University, Bloomington 47405.
Morse
D P
DP
Brown
J W
JW
Schmidt
F J
FJ
Pace
N R
NR
D001412:Bacillus subtilis / Q000201:enzymology / Q000235:genetics; D001482:Base Composition; D001483:Base Sequence; D005075:Biological Evolution; D004722:Endoribonucleases / Q000235:genetics*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016296:Mutagenesis; D009690:Nucleic Acid Conformation; D012329:RNA, Bacterial / Q000235:genetics*; D016337:RNA, Catalytic / Q000235:genetics*; D043262:Ribonuclease P
D029968:Escherichia coli Proteins; D012329:RNA, Bacterial; D016337:RNA, Catalytic; D004722:Endoribonucleases; D043262:Ribonuclease P; C470865:ribonuclease P, E coli