Similar cage-shaped structures for the RNA components of all ribonuclease P and ribonuclease MRP enzymes.
Department of Biology, Yale University, New Haven, Connecticut 06520.
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Forster
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Altman
D001412:Bacillus subtilis / Q000235:genetics; D001483:Base Sequence; D004722:Endoribonucleases / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D005800:Genes, Fungal; D006367:HeLa Cells / Q000032:analysis; D006801:Humans; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D012329:RNA, Bacterial / Q000235:genetics*; D043262:Ribonuclease P; D012441:Saccharomyces cerevisiae / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid
D029968:Escherichia coli Proteins; D012329:RNA, Bacterial; D004722:Endoribonucleases; C058330:mitochondrial RNA-processing endoribonuclease; C468368:RPP14 protein, human; D043262:Ribonuclease P; C470865:ribonuclease P, E coli