Human ribonuclease P: subunits, function, and intranuclear localization.
Catalytic complexes of nuclear ribonuclease P (RNase P) ribonucleoproteins are composed of several protein subunits that appear to have specific roles in enzyme function in tRNA processing. This review describes recent progress made in the characterization of human RNase P, its relationship with the ribosomal RNA processing ribonucleoprotein RNase MRP, and the unexpected evolutionary conservation of its subunits. A new model for the biosynthesis of human RNase P is presented, in which this process is dynamic, transcription-dependent, and implicates functionally distinct nuclear compartments in tRNA biogenesis.
Jarrous
Nayef
N
Department of Molecular Biology, The Hebrew University-Hadassah Medical School, Jerusalem, Israel. jarrous@md.huji.ac.il
D002467:Cell Nucleus / Q000378:metabolism*; D017124:Conserved Sequence; D004722:Endoribonucleases / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D046911:Macromolecular Substances; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D021122:Protein Subunits; D016337:RNA, Catalytic / Q000737:chemistry* / Q000378:metabolism*; D043262:Ribonuclease P; D012261:Ribonucleoproteins / Q000378:metabolism
D046911:Macromolecular Substances; D021122:Protein Subunits; D016337:RNA, Catalytic; D012261:Ribonucleoproteins; D004722:Endoribonucleases; C058330:mitochondrial RNA-processing endoribonuclease; C468368:RPP14 protein, human; D043262:Ribonuclease P