title: Function and subnuclear distribution of Rpp21, a protein subunit of the human ribonucleoprotein ribonuclease P.
abstract: Rpp21, a protein subunit of human nuclear ribonuclease P (RNase P) was cloned by virtue of its homology with Rpr2p, an essential subunit of Saccharomyces cerevisiae nuclear RNase P. Rpp21 is encoded by a gene that resides in the class I gene cluster of the major histocompatibility complex, is associated with highly purified RNase P, and binds precursor tRNA. Rpp21 is predominantly localized in the nucleoplasm but is also observed in nucleoli and Cajal bodies when expressed at high levels. Intron retention and splice-site selection in Rpp21 precursor mRNA regulate the intranuclear distribution of the protein products and their association with the RNase P holoenzyme. Our study reveals that dynamic nuclear structures that include nucleoli, the perinucleolar compartment and Cajal bodies are all involved in the production and assembly of human RNase P.
authors.affiliation: Department of Molecular Biology, The Hebrew University-Hadassah Medical School, Jerusalem, Israel. jarrous@md.huji.ac.il
authors.forename: N
authors.initials: N
authors.lastname: Jarrous
authors.forename: R
authors.initials: R
authors.lastname: Reiner
authors.forename: D
authors.initials: D
authors.lastname: Wesolowski
authors.forename: H
authors.initials: H
authors.lastname: Mann
authors.forename: C
authors.initials: C
authors.lastname: Guerrier-Takada
authors.forename: S
authors.initials: S
authors.lastname: Altman
mesh_terms: D016475:3T3 Cells; D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D002467:Cell Nucleus / Q000737:chemistry / Q000378:metabolism; D002478:Cells, Cultured; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000378:metabolism; D004722:Endoribonucleases / Q000737:chemistry* / Q000378:metabolism; D005347:Fibroblasts / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D007438:Introns; D008285:Major Histocompatibility Complex; D051379:Mice; D008856:Microscopy, Fluorescence; D008957:Models, Genetic; D008969:Molecular Sequence Data; D011233:Precipitin Tests; D011485:Protein Binding; D012326:RNA Splicing; D016337:RNA, Catalytic / Q000737:chemistry* / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D012343:RNA, Transfer / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D043262:Ribonuclease P; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid
chemical_list: D018076:DNA, Complementary; D016337:RNA, Catalytic; D012333:RNA, Messenger; D011994:Recombinant Proteins; D012343:RNA, Transfer; D004722:Endoribonucleases; C468368:RPP14 protein, human; D043262:Ribonuclease P