Non-coding RNAs: lessons from the small nuclear and small nucleolar RNAs (original) (raw)
Cheng, J. et al. Transcriptional maps of 10 human chromosomes at 5-nucleotide resolution. Science308, 1149–1154 (2005). CASPubMed Google Scholar
Mattick, J. S. & Makunin, I. V. Non-coding RNA. Hum. Mol. Genet.15, R17–R29 (2006). CASPubMed Google Scholar
Huttenhofer, A., Schattner, P. & Polacek, N. Non-coding RNAs: hope or hype? Trends Genet.21, 289–297 (2005). PubMed Google Scholar
Storz, G., Altuvia, S. & Wassarman, K. M. An abundance of RNA regulators. Annu. Rev. Biochem.74, 199–217 (2005). CASPubMed Google Scholar
Szymanski, M., Barciszewska, M. Z., Zywicki, M. & Barciszewski, J. Noncoding RNA transcripts. J. Appl. Genet.44, 1–19 (2003). PubMed Google Scholar
Eddy, S. R. Computational genomics of noncoding RNA genes. Cell109, 137–140 (2002). CASPubMed Google Scholar
Goodrich, J. A. & Kugel, J. F. Non-coding-RNA regulators of RNA polymerase II transcription. Nature Rev. Mol. Cell Biol.7, 612–616 (2006). CAS Google Scholar
Huttenhofer, A. & Schattner, P. The principles of guiding by RNA: chimeric RNA–protein enzymes. Nature Rev. Genet.7, 475–482 (2006). PubMed Google Scholar
Valadkhan, S. snRNAs as the catalysts of pre-mRNA splicing. Curr. Opin. Chem. Biol.9, 603–608 (2005). CASPubMed Google Scholar
Will, C. L. & Luhrmann, R. in The RNA World 3rd edn (eds Gesteland, R. F., Cech, T. R. & Atkins, A. J.) 369–400 (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, 2006). Google Scholar
Nilsen, T. W. The spliceosome: the most complex macromolecular machine in the cell? Bioessays25, 1147–1149 (2003). PubMed Google Scholar
Hernandez, N. Small nuclear RNA genes: a model system to study fundamental mechanisms of transcription. J. Biol. Chem.276, 26733–26736 (2001). CASPubMed Google Scholar
Hernandez, N. & Weiner, A. M. Formation of the 3′ end of U1 snRNA requires compatible snRNA promoter elements. Cell47, 249–258 (1986). CASPubMed Google Scholar
de Vegvar, H. E., Lund, E. & Dahlberg, J. E. 3′ end formation of U1 snRNA precursors is coupled to transcription from snRNA promoters. Cell47, 259–266 (1986). CASPubMed Google Scholar
Baillat, D. et al. Integrator, a multiprotein mediator of small nuclear RNA processing, associates with the C-terminal repeat of RNA polymerase II. Cell123, 265–276 (2005). These authors purified a long-sought complex required for 3′-end processing of pre-snRNA transcripts. CASPubMed Google Scholar
Dominski, Z., Yang, X. C. & Marzluff, W. F. The polyadenylation factor CPSF-73 is involved in histone-pre-mRNA processing. Cell123, 37–48 (2005). CASPubMed Google Scholar
Kolev, N. G. & Steitz, J. A. Symplekin and multiple other polyadenylation factors participate in 3′-end maturation of histone mRNAs. Genes Dev.19, 2583–2592 (2005). Together with reference 16, showed that core factors involved in mRNA polyadenylation form distinct complexes that are required for proper histone 3′-end maturation. CASPubMedPubMed Central Google Scholar
Steinmetz, E. J., Conrad, N. K., Brow, D. A. & Corden, J. L. RNA-binding protein Nrd1 directs poly(A)-independent 3′-end formation of RNA polymerase II transcripts. Nature413, 327–331 (2001). The first paper to recognize the role of Nrd1 in preventing read-through transcription of non-polyadenylated snRNA and snoRNA genes in yeast. CASPubMed Google Scholar
Carroll, K. L., Pradhan, D. A., Granek, J. A., Clarke, N. D. & Corden, J. L. Identification of cis elements directing termination of yeast nonpolyadenylated snoRNA transcripts. Mol. Cell. Biol.24, 6241–6252 (2004). CASPubMedPubMed Central Google Scholar
Steinmetz, E. J., Ng, S. B., Cloute, J. P. & Brow, D. A. _cis_- and _trans_-acting determinants of transcription termination by yeast RNA polymerase II. Mol. Cell. Biol.26, 2688–2696 (2006). CASPubMedPubMed Central Google Scholar
Sheldon, K. E., Mauger, D. M. & Arndt, K. M. A requirement for the Saccharomyces cerevisiae Paf1 complex in snoRNA 3′ end formation. Mol. Cell20, 225–236 (2005). CASPubMedPubMed Central Google Scholar
Thiebaut, M., Kisseleva-Romanova, E., Rougemaille, M., Boulay, J. & Libri, D. Transcription termination and nuclear degradation of cryptic unstable transcripts: a role for the Nrd1–Nab3 pathway in genome surveillance. Mol. Cell23, 853–864 (2006). CASPubMed Google Scholar
Arigo, J. T., Eyler, D. E., Carroll, K. L. & Corden, J. L. Termination of cryptic unstable transcripts is directed by yeast RNA-binding proteins Nrd1 and Nab3. Mol. Cell23, 841–851 (2006). CASPubMed Google Scholar
Schramm, L. & Hernandez, N. Recruitment of RNA polymerase III to its target promoters. Genes Dev.16, 2593–2620 (2002). CASPubMed Google Scholar
Ohno, M., Segref, A., Bachi, A., Wilm, M. & Mattaj, I. W. PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation. Cell101, 187–198 (2000). CASPubMed Google Scholar
Segref, A., Mattaj, I. W. & Ohno, M. The evolutionarily conserved region of the U snRNA export mediator PHAX is a novel RNA-binding domain that is essential for U snRNA export. RNA7, 351–360 (2001). CASPubMedPubMed Central Google Scholar
Ohno, M., Segref, A., Kuersten, S. & Mattaj, I. W. Identity elements used in export of mRNAs. Mol. Cell9, 659–671 (2002). CASPubMed Google Scholar
Masuyama, K., Taniguchi, I., Kataoka, N. & Ohno, M. RNA length defines RNA export pathway. Genes Dev.18, 2074–2085 (2004). CASPubMedPubMed Central Google Scholar
Terns, M. P. & Dahlberg, J. E. Retention and 5′ cap trimethylation of U3 snRNA in the nucleus. Science264, 959–961 (1994). CASPubMed Google Scholar
Boulon, S. et al. PHAX and CRM1 are required sequentially to transport U3 snoRNA to nucleoli. Mol. Cell16, 777–787 (2004). CASPubMed Google Scholar
Watkins, N. J. et al. Assembly and maturation of the U3 snoRNP in the nucleoplasm in a large dynamic multiprotein complex. Mol. Cell16, 789–798 (2004). CASPubMed Google Scholar
Terns, M. P., Grimm, C., Lund, E. & Dahlberg, J. E. A common maturation pathway for small nucleolar RNAs. EMBO J.14, 4860–4871 (1995). CASPubMedPubMed Central Google Scholar
Speckmann, W., Narayanan, A., Terns, R. & Terns, M. P. Nuclear retention elements of U3 small nucleolar RNA. Mol. Cell. Biol.19, 8412–8421 (1999). CASPubMedPubMed Central Google Scholar
Smith, K. P. & Lawrence, J. B. Interactions of U2 gene loci and their nuclear transcripts with Cajal (coiled) bodies: evidence for PreU2 within Cajal bodies. Mol. Biol. Cell11, 2987–2998 (2000). CASPubMedPubMed Central Google Scholar
Matera, A. G. & Shpargel, K. B. Pumping RNA: nuclear bodybuilding along the RNP pipeline. Curr. Opin. Cell Biol.18, 317–324 (2006). CASPubMed Google Scholar
Terns, M. P. & Terns, R. M. Macromolecular complexes: SMN — the master assembler. Curr. Biol.11, R862–R864 (2001). CASPubMed Google Scholar
Eggert, C., Chari, A., Laggerbauer, B. & Fischer, U. Spinal muscular atrophy: the RNP connection. Trends Mol. Med.12, 113–121 (2006). CASPubMed Google Scholar
Golembe, T. J., Yong, J. & Dreyfuss, G. Specific sequence features, recognized by the SMN complex, identify snRNAs and determine their fate as snRNPs. Mol. Cell. Biol.25, 10989–11004 (2005). CASPubMedPubMed Central Google Scholar
Battle, D. J. et al. The Gemin5 protein of the SMN complex identifies snRNAs. Mol. Cell23, 273–279 (2006). CASPubMed Google Scholar
Pillai, R. S. et al. Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing. Genes Dev.17, 2321–2333 (2003). Showed that LSM11 replaces SmD2 in the U7 core and demonstrated the existence of a distinct pool of SMN complexes that lack the canonical SmD1 and SmD2, but that contain LSM10 and LSM11. CASPubMedPubMed Central Google Scholar
Mouaikel, J., Verheggen, C., Bertrand, E., Tazi, J. & Bordonne, R. Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus. Mol. Cell9, 891–901 (2002). Identified the 5′-cap hypermethylase Tgs1, the activity of which was later shown to be essential in metazoans. CASPubMed Google Scholar
Huang, Q. & Pederson, T. A human U2 RNA mutant stalled in 3′ end processing is impaired in nuclear import. Nucleic Acids Res.27, 1025–1031 (1999). CASPubMedPubMed Central Google Scholar
Palacios, I., Hetzer, M., Adam, S. A. & Mattaj, I. W. Nuclear import of U snRNPs requires importin β. EMBO J.16, 6783–6792 (1997). CASPubMedPubMed Central Google Scholar
Huber, J. et al. Snurportin1, an m3G-cap-specific nuclear import receptor with a novel domain structure. EMBO J.17, 4114–4126 (1998). CASPubMedPubMed Central Google Scholar
Narayanan, U., Achsel, T., Luhrmann, R. & Matera, A. G. Coupled in vitro import of U snRNPs and SMN, the spinal muscular atrophy protein. Mol. Cell16, 223–234 (2004). Showed that the SMN complex participates in nuclear import as an adaptor between the Sm core and importin-β. CASPubMed Google Scholar
Huber, J., Dickmanns, A. & Luhrmann, R. The importin-β binding domain of snurportin1 is responsible for the Ran- and energy-independent nuclear import of spliceosomal U snRNPs in vitro. J. Cell Biol.156, 467–479 (2002). CASPubMedPubMed Central Google Scholar
Sleeman, J. E. & Lamond, A. I. Newly assembled snRNPs associate with coiled bodies before speckles, suggesting a nuclear snRNP maturation pathway. Curr. Biol.9, 1065–1074 (1999). CASPubMed Google Scholar
Stanek, D., Rader, S. D., Klingauf, M. & Neugebauer, K. M. Targeting of U4/U6 small nuclear RNP assembly factor SART3/p110 to Cajal bodies. J. Cell Biol.160, 505–516 (2003). CASPubMedPubMed Central Google Scholar
Nesic, D., Tanackovic, G. & Kramer, A. A role for Cajal bodies in the final steps of U2 snRNP biogenesis. J. Cell Sci.117, 4423–4433 (2004). CASPubMed Google Scholar
Schaffert, N., Hossbach, M., Heintzmann, R., Achsel, T. & Luhrmann, R. RNAi knockdown of hPrp31 leads to an accumulation of U4/U6 di-snRNPs in Cajal bodies. EMBO J.23, 3000–3009 (2004). CASPubMedPubMed Central Google Scholar
Stanek, D. & Neugebauer, K. M. Detection of snRNP assembly intermediates in Cajal bodies by fluorescence resonance energy transfer. J. Cell Biol.166, 1015–1025 (2004). CASPubMedPubMed Central Google Scholar
Tanackovic, G. & Kramer, A. Human splicing factor SF3a, but not SF1, is essential for pre-mRNA splicing in vivo. Mol. Biol. Cell16, 1366–1377 (2005). CASPubMedPubMed Central Google Scholar
Lestrade, L. & Weber, M. J. snoRNA-LBME-db, a comprehensive database of human H/ACA and C/D box snoRNAs. Nucleic Acids Res.34, D158–D162 (2006). CASPubMed Google Scholar
Kiss, T. Small nucleolar RNAs: an abundant group of noncoding RNAs with diverse cellular functions. Cell109, 145–148 (2002). CASPubMed Google Scholar
Henras, A. K., Dez, C. & Henry, Y. RNA structure and function in C/D and H/ACA s(no)RNPs. Curr. Opin. Struct. Biol.14, 335–343 (2004). CASPubMed Google Scholar
Terns, M. P. & Terns, R. M. Small nucleolar RNAs: versatile _trans_-acting molecules of ancient evolutionary origin. Gene Expr.10, 17–39 (2002). CASPubMed Google Scholar
Yu, Y. T., Terns, R. M. & Terns, M. P. in Fine-tuning of RNA Functions by Modification and Editing Vol. 12 (ed. Grosjean, H.) 223–262 (Topics in Current Genetics, New York, 2005). Google Scholar
Decatur, W. A. & Fournier, M. J. RNA-guided nucleotide modification of ribosomal and other RNAs. J. Biol. Chem.278, 695–698 (2003). CASPubMed Google Scholar
Darzacq, X. et al. Cajal body-specific small nuclear RNAs: a novel class of 2′-_O_-methylation and pseudouridylation guide RNAs. EMBO J.21, 2746–2756 (2002). Identified scaRNAs as modification-guide RNAs that localize in Cajal bodies. CASPubMedPubMed Central Google Scholar
Dennis, P. P., Omer, A. & Lowe, T. A guided tour: small RNA function in Archaea. Mol. Microbiol.40, 509–519 (2001). CASPubMed Google Scholar
Uliel, S., Liang, X. H., Unger, R. & Michaeli, S. Small nucleolar RNAs that guide modification in trypanosomatids: repertoire, targets, genome organisation, and unique functions. Int. J. Parasitol.34, 445–454 (2004). CASPubMed Google Scholar
Cavaille, J. et al. Identification of brain-specific and imprinted small nucleolar RNA genes exhibiting an unusual genomic organization. Proc. Natl Acad. Sci. USA97, 14311–14316 (2000). CASPubMedPubMed Central Google Scholar
Vitali, P. et al. ADAR2-mediated editing of RNA substrates in the nucleolus is inhibited by C/D small nucleolar RNAs. J. Cell Biol.169, 745–753 (2005). CASPubMedPubMed Central Google Scholar
Kishore, S. & Stamm, S. The snoRNA HBII-52 regulates alternative splicing of the serotonin receptor 2C. Science311, 230–232 (2006). CASPubMed Google Scholar
Collins, K. The biogenesis and regulation of telomerase holoenzymes. Nature Rev. Mol. Cell Biol.7, 484–494 (2006). CAS Google Scholar
Huttenhofer, A. et al. RNomics: an experimental approach that identifies 201 candidates for novel, small, non-messenger RNAs in mouse. EMBO J.20, 2943–2953 (2001). CASPubMedPubMed Central Google Scholar
Kiss, A. M., Jady, B. E., Bertrand, E. & Kiss, T. Human box H/ACA pseudouridylation guide RNA machinery. Mol. Cell. Biol.24, 5797–5807 (2004). CASPubMedPubMed Central Google Scholar
Omer, A. D., Ziesche, S., Ebhardt, H. & Dennis, P. P. In vitro reconstitution and activity of a C/D box methylation guide ribonucleoprotein complex. Proc. Natl Acad. Sci. USA99, 5289–5294 (2002). Established the essential components of the C/D RNP and its hierarchical assembly pathway. CASPubMedPubMed Central Google Scholar
Bortolin, M. L., Bachellerie, J. P. & Clouet-d'Orval, B. In vitro RNP assembly and methylation guide activity of an unusual box C/D RNA, _cis_-acting archaeal pre-tRNA(Trp). Nucleic Acids Res.31, 6524–6535 (2003). CASPubMedPubMed Central Google Scholar
Rashid, R. et al. Functional requirement for symmetric assembly of archaeal box C/D small ribonucleoprotein particles. J. Mol. Biol.333, 295–306 (2003). CASPubMed Google Scholar
Tran, E. J., Zhang, X. & Maxwell, E. S. Efficient RNA 2′-_O_-methylation requires juxtaposed and symmetrically assembled archaeal box C/D and C′/D′ RNPs. EMBO J.22, 3930–3940 (2003). CASPubMedPubMed Central Google Scholar
Baker, D. L. et al. RNA-guided RNA modification: functional organization of the archaeal H/ACA RNP. Genes Dev.19, 1238–1248 (2005). CASPubMedPubMed Central Google Scholar
Charpentier, B., Muller, S. & Branlant, C. Reconstitution of archaeal H/ACA small ribonucleoprotein complexes active in pseudouridylation. Nucleic Acids Res.33, 3133–3144 (2005). References 75 and 76 defined the essential components and organization of the H/ACA RNP. CASPubMedPubMed Central Google Scholar
Wang, H., Boisvert, D., Kim, K. K., Kim, R. & Kim, S. H. Crystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 Å resolution. EMBO J.19, 317–323 (2000). CASPubMedPubMed Central Google Scholar
Deng, L. et al. Structure determination of fibrillarin from the hyperthermophilic archaeon Pyrococcus furiosus. Biochem. Biophys. Res. Commun.315, 726–732 (2004). CASPubMed Google Scholar
Aittaleb, M. et al. Structure and function of archaeal box C/D sRNP core proteins. Nature Struct. Biol.10, 256–263 (2003). Provided insight into the structure and organization of a key subcomplex of the C/D RNP. CASPubMed Google Scholar
Suryadi, J., Tran, E. J., Maxwell, E. S. & Brown, B. A. 2nd. The crystal structure of the Methanocaldococcus jannaschii multifunctional L7Ae RNA-binding protein reveals an induced-fit interaction with the box C/D RNAs. Biochemistry44, 9657–9672 (2005). CASPubMed Google Scholar
Moore, T., Zhang, Y., Fenley, M. O. & Li, H. Molecular basis of box C/D RNA-protein interactions; cocrystal structure of archaeal L7Ae and a box C/D RNA. Structure12, 807–818 (2004). CASPubMed Google Scholar
Rashid, R. et al. Crystal structure of a Cbf5–Nop10–Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita. Mol. Cell21, 249–260 (2006). CASPubMed Google Scholar
Manival, X. et al. Crystal structure determination and site-directed mutagenesis of the Pyrococcus abyssi aCBF5–aNOP10 complex reveal crucial roles of the C-terminal domains of both proteins in H/ACA sRNP activity. Nucleic Acids Res.34, 826–839 (2006). CASPubMedPubMed Central Google Scholar
Hamma, T., Reichow, S. L., Varani, G. & Ferre-D'Amare, A. R. The Cbf5–Nop10 complex is a molecular bracket that organizes box H/ACA RNPs. Nature Struct. Mol. Biol.12, 1101–1107 (2005). CAS Google Scholar
Hamma, T. & Ferre-D'Amare, A. R. Structure of protein L7Ae bound to a K-turn derived from an archaeal box H/ACA sRNA at 1.8 Å resolution. Structure12, 893–903 (2004). CASPubMed Google Scholar
Li, L. & Ye, K. Crystal structure of an H/ACA box ribonucleoprotein particle. Nature443, 302–307 (2006). References 82 and 86 describe the crystal structures of H/ACA RNP complexes and provide insight into the molecular basis of dyskeratosis congenita. CASPubMed Google Scholar
Mitchell, J. R., Wood, E. & Collins, K. A telomerase component is defective in the human disease dyskeratosis congenita. Nature402, 551–555 (1999). CASPubMed Google Scholar
Mochizuki, Y., He, J., Kulkarni, S., Bessler, M. & Mason, P. J. Mouse dyskerin mutations affect accumulation of telomerase RNA and small nucleolar RNA, telomerase activity, and ribosomal RNA processing. Proc. Natl Acad. Sci. USA101, 10756–10761 (2004). CASPubMedPubMed Central Google Scholar
Marrone, A., Walne, A. & Dokal, I. Dyskeratosis congenita: telomerase, telomeres and anticipation. Curr. Opin. Genet. Dev.15, 249–257 (2005). CASPubMed Google Scholar
Watkins, N. J. et al. Cbf5p, a potential pseudouridine synthase, and Nhp2p, a putative RNA-binding protein, are present together with Gar1p in all H BOX/ACA-motif snoRNPs and constitute a common bipartite structure. RNA4, 1549–1568 (1998). CASPubMedPubMed Central Google Scholar
Wang, C., Query, C. C. & Meier, U. T. Immunopurified small nucleolar ribonucleoprotein particles pseudouridylate rRNA independently of their association with phosphorylated Nopp140. Mol. Cell. Biol.22, 8457–8466 (2002). CASPubMedPubMed Central Google Scholar
Henras, A. K., Capeyrou, R., Henry, Y. & Caizergues-Ferrer, M. Cbf5p, the putative pseudouridine synthase of H/ACA-type snoRNPs, can form a complex with Gar1p and Nop10p in absence of Nhp2p and box H/ACA snoRNAs. RNA10, 1704–1712 (2004). CASPubMedPubMed Central Google Scholar
Schultz, A., Nottrott, S., Watkins, N. J. & Luhrmann, R. Protein–protein and protein–RNA contacts both contribute to the 15.5K-mediated assembly of the U4/U6 snRNP and the box C/D snoRNPs. Mol. Cell. Biol.26, 5146–5154 (2006). CASPubMedPubMed Central Google Scholar
Szewczak, L. B., DeGregorio, S. J., Strobel, S. A. & Steitz, J. A. Exclusive interaction of the 15.5 kD protein with the terminal box C/D motif of a methylation guide snoRNP. Chem. Biol.9, 1095–1107 (2002). CASPubMed Google Scholar
Darzacq, X. et al. Stepwise RNP assembly at the site of H/ACA RNA transcription in human cells. J. Cell Biol.173, 207–218 (2006). CASPubMedPubMed Central Google Scholar
Ballarino, M., Morlando, M., Pagano, F., Fatica, A. & Bozzoni, I. The cotranscriptional assembly of snoRNPs controls the biosynthesis of H/ACA snoRNAs in Saccharomyces cerevisiae. Mol. Cell. Biol.25, 5396–5403 (2005). CASPubMedPubMed Central Google Scholar
Yang, P. K. et al. Cotranscriptional recruitment of the pseudouridylsynthetase Cbf5p and of the RNA binding protein Naf1p during H/ACA snoRNP assembly. Mol. Cell. Biol.25, 3295–3304 (2005). References 95 and 97 provided detailed evidence for the current model of co-transcriptional assembly of inactive pre-H/ACA RNPs, including the role of exchange factors. CASPubMedPubMed Central Google Scholar
Richard, P., Kiss, A. M., Darzacq, X. & Kiss, T. Cotranscriptional recognition of human intronic box H/ACA snoRNAs occurs in a splicing-independent manner. Mol. Cell. Biol.26, 2540–2549 (2006). CASPubMedPubMed Central Google Scholar
Yang, P. K., Rotondo, G., Porras, T., Legrain, P. & Chanfreau, G. The Shq1p–Naf1p complex is required for box H/ACA small nucleolar ribonucleoprotein particle biogenesis. J. Biol. Chem.277, 45235–45242 (2002). CASPubMed Google Scholar
Dez, C., Noaillac-Depeyre, J., Caizergues-Ferrer, M. & Henry, Y. Naf1p, an essential nucleoplasmic factor specifically required for accumulation of box H/ACA small nucleolar RNPs. Mol. Cell. Biol.22, 7053–7065 (2002). CASPubMedPubMed Central Google Scholar
Hoareau-Aveilla, C., Bonoli, M., Caizergues-Ferrer, M. & Henry, Y. hNaf1 is required for accumulation of human box H/ACA snoRNPs, scaRNPs, and telomerase. RNA12, 832–840 (2006). CASPubMedPubMed Central Google Scholar
Morlando, M. et al. Coupling between snoRNP assembly and 3′ processing controls box C/D snoRNA biosynthesis in yeast. EMBO J.23, 2392–2401 (2004). CASPubMedPubMed Central Google Scholar
Hirose, T. & Steitz, J. A. Position within the host intron is critical for efficient processing of box C/D snoRNAs in mammalian cells. Proc. Natl Acad. Sci. USA98, 12914–12919 (2001). CASPubMedPubMed Central Google Scholar
Verheggen, C. et al. Mammalian and yeast U3 snoRNPs are matured in specific and related nuclear compartments. EMBO J.21, 2736–2745 (2002). CASPubMedPubMed Central Google Scholar
Hirose, T., Shu, M. D. & Steitz, J. A. Splicing-dependent and-independent modes of assembly for intron-encoded box C/D snoRNPs in mammalian cells. Mol. Cell12, 113–123 (2003). CASPubMed Google Scholar
Hirose, T. et al. A spliceosomal intron binding protein, IBP160, links position-dependent assembly of intron-encoded box C/D snoRNP to pre-mRNA splicing. Mol. Cell23, 673–684 (2006). CASPubMed Google Scholar
Peng, W. T. et al. A panoramic view of yeast noncoding RNA processing. Cell113, 919–933 (2003). CASPubMed Google Scholar
Hiley, S. L., Babak, T. & Hughes, T. R. Global analysis of yeast RNA processing identifies new targets of RNase III and uncovers a link between tRNA 5′ end processing and tRNA splicing. Nucleic Acids Res.33, 3048–3056 (2005). CASPubMedPubMed Central Google Scholar
Houseley, J., LaCava, J. & Tollervey, D. RNA-quality control by the exosome. Nature Rev. Mol. Cell Biol.7, 529–539 (2006). CAS Google Scholar
LaCava, J. et al. RNA degradation by the exosome is promoted by a nuclear polyadenylation complex. Cell121, 713–724 (2005). CASPubMed Google Scholar
Vasiljeva, L. & Buratowski, S. Nrd1 interacts with the nuclear exosome for 3′ processing of RNA polymerase II transcripts. Mol. Cell21, 239–248 (2006). CASPubMed Google Scholar
King, T. H., Decatur, W. A., Bertrand, E., Maxwell, E. S. & Fournier, M. J. A well-connected and conserved nucleoplasmic helicase is required for production of box C/D and H/ACA snoRNAs and localization of snoRNP proteins. Mol. Cell. Biol.21, 7731–7746 (2001). CASPubMedPubMed Central Google Scholar
Samarsky, D. A., Fournier, M. J., Singer, R. H. & Bertrand, E. The snoRNA box C/D motif directs nucleolar targeting and also couples snoRNA synthesis and localization. EMBO J.17, 3747–3757 (1998). CASPubMedPubMed Central Google Scholar
Richard, P. et al. A common sequence motif determines the Cajal body-specific localization of box H/ACA scaRNAs. EMBO J.22, 4283–4293 (2003). CASPubMedPubMed Central Google Scholar
Narayanan, A., Speckmann, W., Terns, R. & Terns, M. P. Role of the box C/D motif in localization of small nucleolar RNAs to coiled bodies and nucleoli. Mol. Biol. Cell10, 2131–2147 (1999). CASPubMedPubMed Central Google Scholar
Gall, J. G. The centennial of the Cajal body. Nature Rev. Mol. Cell Biol.4, 975–980 (2003). CAS Google Scholar
Cioce, M. & Lamond, A. I. Cajal bodies: a long history of discovery. Annu. Rev. Cell. Dev. Biol.21, 105–131 (2005). CASPubMed Google Scholar
Gubitz, A. K., Feng, W. & Dreyfuss, G. The SMN complex. Exp. Cell Res.296, 51–56 (2004). CASPubMed Google Scholar
Whitehead, S. E. et al. Determinants of the interaction of the spinal muscular atrophy disease protein SMN with the dimethylarginine-modified box H/ACA small nucleolar ribonucleoprotein GAR1. J. Biol. Chem.277, 48087–48093 (2002). CASPubMed Google Scholar
Pellizzoni, L., Baccon, J., Charroux, B. & Dreyfuss, G. The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1. Curr. Biol.11, 1079–1088 (2001). CASPubMed Google Scholar
Jones, K. W. et al. Direct interaction of the spinal muscular atrophy disease protein SMN with the small nucleolar RNA-associated protein fibrillarin. J. Biol. Chem.276, 38645–38651 (2001). CASPubMed Google Scholar
Narayanan, A. et al. Nucleolar localization signals of box H/ACA small nucleolar RNAs. EMBO J.18, 5120–5130 (1999). CASPubMedPubMed Central Google Scholar
Lange, T. S., Ezrokhi, M., Amaldi, F. & Gerbi, S. A. Box H and box ACA are nucleolar localization elements of U17 small nucleolar RNA. Mol. Biol. Cell10, 3877–3890 (1999). CASPubMedPubMed Central Google Scholar
Jady, B. E., Bertrand, E. & Kiss, T. Human telomerase RNA and box H/ACA scaRNAs share a common Cajal body-specific localization signal. J. Cell Biol.164, 647–652 (2004). CASPubMedPubMed Central Google Scholar
Fu, D. & Collins, K. Human telomerase and Cajal body ribonucleoproteins share a unique specificity of Sm protein association. Genes Dev.20, 531–536 (2006). CASPubMedPubMed Central Google Scholar
Tomlinson, R. L., Ziegler, T. D., Supakorndej, T., Terns, R. M. & Terns, M. P. Cell cycle-regulated trafficking of human telomerase to telomeres. Mol. Biol. Cell17, 955–965 (2006). CASPubMedPubMed Central Google Scholar
Jady, B. E., Richard, P., Bertrand, E. & Kiss, T. Cell cycle-dependent recruitment of telomerase RNA and Cajal bodies to human telomeres. Mol. Biol. Cell17, 944–954 (2006). References 127 and 128 revealed that trafficking of the human telomerase RNP is regulated as a function of the cell cycle. CASPubMedPubMed Central Google Scholar
Seto, A. G., Zaug, A. J., Sobel, S. G., Wolin, S. L. & Cech, T. R. Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle. Nature401, 177–180 (1999). CASPubMed Google Scholar
Li, C. F. et al. An ARGONAUTE4-containing nuclear processing center colocalized with Cajal bodies in Arabidopsis thaliana. Cell126, 93–106 (2006). CASPubMed Google Scholar
Pontes, O. et al. The Arabidopsis chromatin-modifying nuclear siRNA pathway involves a nucleolar RNA processing center. Cell126, 79–92 (2006). CASPubMed Google Scholar
Briese, M., Esmaeili, B. & Sattelle, D. B. Is spinal muscular atrophy the result of defects in motor neuron processes? Bioessays27, 946–957 (2005). CASPubMed Google Scholar
Wattendorf, D. J. & Muenke, M. Prader–Willi syndrome. Am. Fam. Physician72, 827–830 (2005). PubMed Google Scholar
Cahill, N. M. et al. Site-specific cross-linking analyses reveal an asymmetric protein distribution for a box C/D snoRNP. EMBO J.21, 3816–3828 (2002). CASPubMedPubMed Central Google Scholar
Filipowicz, W. & Pogacic, V. Biogenesis of small nucleolar ribonucleoproteins. Curr. Opin. Cell Biol.14, 319–327 (2002). CASPubMed Google Scholar
Eliassen, K. A., Baldwin, A., Sikorski, E. M. & Hurt, M. M. Role for a YY1-binding element in replication-dependent mouse histone gene expression. Mol. Cell. Biol.18, 7106–7118 (1998). CASPubMedPubMed Central Google Scholar