Structure-function analysis in nuclear RNase P RNA.
Eukaryotic ribonuclease P (RNase P) enzymes require both RNA and protein subunits for activity in vivo and in vitro. We have undertaken an analysis of the complex RNA subunit of the nuclear holoenzyme in an effort to understand its structure and its similarities to and differences from the bacterial ribozymes. Phylogenetic analysis, structure-sensitive RNA footprinting, and directed mutagenesis reveal conserved secondary and tertiary structures with both strong similarities to the bacterial consensus and distinctive features. The effects of mutations in the most highly conserved positions are being used to dissect the functions of individual subdomains.
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109-0606, USA.
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Engelke
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Pagán-Ramos
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Tranguch
D001419:Bacteria / Q000201:enzymology; D001483:Base Sequence; D002467:Cell Nucleus / Q000378:metabolism; D016384:Consensus Sequence; D004722:Endoribonucleases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D014644:Genetic Variation; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009690:Nucleic Acid Conformation; D010802:Phylogeny; D016337:RNA, Catalytic / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D043262:Ribonuclease P; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D012568:Schizosaccharomyces / Q000201:enzymology
D016337:RNA, Catalytic; D004722:Endoribonucleases; D043262:Ribonuclease P