Eukaryotic ribonuclease P: increased complexity to cope with the nuclear pre-tRNA pathway.
Ribonuclease P is an ancient enzyme that cleaves pre-tRNAs to generate mature 5' ends. It contains an essential RNA subunit in Bacteria, Archaea, and Eukarya, but the degree to which the RNA subunit relies on proteins to supplement catalysis is highly variable. The eukaryotic nuclear holoenzyme has recently been found to contain almost twenty times the protein content of the bacterial enzymes, in addition to having split into at least two related enzymes with distinct substrate specificity. In this review, recent progress in understanding the molecular architecture and functions of nuclear forms of RNase P will be considered.
Department of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan 48109-0606 USA.
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Engelke
D000818:Animals; D005075:Biological Evolution; D002467:Cell Nucleus / Q000201:enzymology / Q000235:genetics; D004722:Endoribonucleases / Q000737:chemistry* / Q000502:physiology*; D046911:Macromolecular Substances; D009690:Nucleic Acid Conformation; D012322:RNA Precursors / Q000378:metabolism; D012323:RNA Processing, Post-Transcriptional; D016337:RNA, Catalytic / Q000737:chemistry* / Q000502:physiology*; D012343:RNA, Transfer / Q000378:metabolism*; D043262:Ribonuclease P; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics; D013379:Substrate Specificity
D046911:Macromolecular Substances; D012322:RNA Precursors; D016337:RNA, Catalytic; D012343:RNA, Transfer; D004722:Endoribonucleases; C058330:mitochondrial RNA-processing endoribonuclease; D043262:Ribonuclease P