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Assembly of Signal Recognition Particles in the Nucleolus

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The Nucleolus

Part of the book series: Protein Reviews ((PRON,volume 15))

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Abstract

In addition to its role in ribosome biogenesis, the nucleolus contributes to many other activities including the processing and assembly of other nonribosomal RNA–protein complexes. Recent findings suggest that the nucleolus is involved in the biogenesis of the signal recognition particle (SRP), a cytoplasmic ribonucleoprotein (RNP) complex that recognizes and targets select ribosomes to the endoplasmic reticulum membrane for the cotranslational translocation of membrane and secretory proteins. Assembly of the SRP into a functional RNP complex requires the ordered, sequential association of protein subunits onto the SRP RNA. Here, we will review our current understanding of SRP assembly with a focus on the role the nucleolus plays in SRP biogenesis.

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References

  • Alavian CN, Ritland Politz JC, Lewandowski LB, Powers CM, Pederson T (2004) Nuclear export of signal recognition particle RNA in mammalian cells. Biochem Biophys Res Commun 313:351–355

    Article  PubMed  CAS  Google Scholar 

  • Althoff S, Selinger D, Wise JA (1994) Molecular evolution of SRP cycle components: functional implications. Nucleic Acids Res 22:1933–1947

    Article  PubMed  CAS  Google Scholar 

  • Andersen JS, Lyon CE, Fox AH, Leung AKL, Lam YW, Steen H, Mann M, Lamond AI (2002) Directed proteomic analysis of human nucleolus. Curr Biol 12:1–11

    Article  PubMed  Google Scholar 

  • Boisvert FM, van Koingsbruggen S, Navascues J, Lamond AI (2007) The multifunctional nucleolus. Nat Rev Mol Cell Biol 8:574–585

    Article  PubMed  CAS  Google Scholar 

  • Bui N, Strub K (1999) New insights into signal recognition and elongation arrest activities of the signal recognition particle. Biol Chem 380:135–145

    Article  PubMed  CAS  Google Scholar 

  • Chen Y, Sinha K, Perumal K, Gu J, Reddy R (1998) Accurate 3′ end processing and adenylation of human signal recognition particle RNA and Alu RNA in vitro. J Biol Chem 273:35023–35031

    Article  PubMed  CAS  Google Scholar 

  • Ciufo LF, Brown JD (2000) Nuclear export of yeast signal recognition particle lacking Srp54p by the Xpo1p/Crm1p NES-dependent pathway. Curr Biol 10:1256–1264

    Article  PubMed  CAS  Google Scholar 

  • Collins LJ, Kurland CG, Biggs P, Penny D (2009) The modern RNP world of eukaryotes. J Hered 100:597–604

    Article  PubMed  CAS  Google Scholar 

  • Dreyfus G, Philipson L, Mattaj IW (1988) Ribonucleoprotein particles in cellular processes. J Cell Biol 106:1419–1425

    Article  Google Scholar 

  • Filipowicz W, Pogacic V (2002) Biogenesis of small nucleolar ribonucleoproteins. Curr Opin Cell Biol 14:319–327

    Article  PubMed  CAS  Google Scholar 

  • Fromont-Racine M, Senger B, Savcanu CFF (2003) Ribosome assembly in eukaryotes. Gene 313:17–42

    Article  PubMed  CAS  Google Scholar 

  • Gadal O, Strauss D, Kessl J, Truppower B, Tollervey D, Hurt E (2001) Nuclear export of 60S ribosomal subunits depends on Xpo1p and requires a nuclear export sequence-containing factor, Nmd3p, that associates with the large subunit protein Rpl10p. Mol Cell Biol 21:3405–3415

    Article  PubMed  CAS  Google Scholar 

  • Gerbi SA, Borovjagin AV, Lang TS (2003) The nucleolus: a site of ribonucleoprotein maturation. Curr Opin Cell Biol 15:318–325

    Article  PubMed  CAS  Google Scholar 

  • Gossen G (1984) Nucleolar structure. Int Rev Cytol 87:107–158

    Google Scholar 

  • Grosshans H, Deinert K, Hurt E, Simos G (2001) Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export. J Cell Biol 153:745–762

    Article  PubMed  CAS  Google Scholar 

  • Gundelfinger ED, Krause E, Melli M, Dobberstein B (1983) The organization of the 7SL RNA component of the signal recognition particle. Nucleic Acids Res 11:7362–7374

    Article  Google Scholar 

  • Ho JH, Kallstrom G, Johnson AW (2000) Nmd3p is a Crm1p-dependent adapter protein for nuclear export of the large ribosomal subunit. J Cell Biol 151:1057–1066

    Article  PubMed  CAS  Google Scholar 

  • Jacobson MR, Pederson T (1997) RNA traffic and localization reported by fluorescent molecular cytochemistry in living cells. In: Richter JD (ed) mRNA formation and function. Academic, New York, pp 341–359

    Chapter  Google Scholar 

  • Jacobson MR, Pederson T (1998) Localization of signal recognition particle RNA in the nucleolus of mammalian cells. Proc Natl Acad Sci USA 95:7981–7986

    Article  PubMed  CAS  Google Scholar 

  • Krieg UC, Walter P, Johnson AE (1986) Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle. Proc Natl Acad Sci USA 83:8604–8608

    Article  PubMed  CAS  Google Scholar 

  • Kurzchalia TV, Wiedmann M, Grischovich AS, Bochkareva ES, Bielka H, Rapoport TA (1986) The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle. Nature 320:634–636

    Article  PubMed  CAS  Google Scholar 

  • Larsen N, Zwieb C (1991) SRP-RNA sequence alignment and secondary structure. Nucleic Acids Res 19:209–215

    Article  PubMed  CAS  Google Scholar 

  • Li WY, Reddy R, Henning D, Epstein P, Busch H (1982) Nucleotide sequence of 7S RNA: homology to ALU DNA and LA 4.5S RNA. J Biol Chem 257:5136–5142

    PubMed  CAS  Google Scholar 

  • Liau MC, Perry RP (1969) Ribosome precursor particles in nucleoli. J Cell Biol 42:272–283

    Article  PubMed  CAS  Google Scholar 

  • Lingelbach K, Zwieb C, Webb JR, Marshallsay C, Hoben PJ, Walter P, Doggerstein B (1998) Isolation and characterization of a cDNA clone encoding the 19 kDa protein of signal recognition particle (SRP): expression and binding to 7SL RNA. Nucleic Acids Res 16:9431–9442

    Article  Google Scholar 

  • Lueng AKI, Lamond AI (2003) The dynamics of the nucleolus. Crit Rev Eukaryot Gene Expr 13:39–54

    Article  Google Scholar 

  • Lutcke H (1995) Signal recognition particle (SRP), a ubiquitous initiator of protein translocation. Eur J Biochem 228:531–550

    Article  PubMed  CAS  Google Scholar 

  • Lutcke H, Prehn S, Ashford AJ, Remus M, Frank R, Dobberstein B (1993) Assembly of the 68- and 72-kD proteins of signal recognition particle with 7S RNA. J Cell Biol 121:977–985

    Article  PubMed  CAS  Google Scholar 

  • Maity TS, Weeks KM (2007) A three-fold RNA-protein interface in the signal recognition particle gates native complex assembly. J Mol Biol 369:512–524

    Article  PubMed  CAS  Google Scholar 

  • Maity TS, Leonard CW, Rose MA, Fried HM, Weeks KM (2006) Compartmentalization directs assembly of the signal recognition particle. Biochemistry 45:14955–14966

    Article  PubMed  CAS  Google Scholar 

  • Maity TS, Fried HM, Weeks KM (2008) Anti-cooperative assembly of the SRP19 and SRP68/72 components of the signal recognition particle. Biochem J 415:429–437

    Article  PubMed  CAS  Google Scholar 

  • Menichelli E, Nagai K (2009) Assembly of the human signal recognition particle. In: Walter NG, Woodson SA, Batey RT (eds) Non-protein coding RNAs. Springer, Berlin, pp 273–284

    Chapter  Google Scholar 

  • Menichelli E, Isel C, Ougridge C, Nagai K (2007) Protein-induced conformational changes of RNA during the assembly of human signal recognition particle. J Mol Biol 367:187–203

    Article  PubMed  CAS  Google Scholar 

  • Mitchell JR, Cheng J, Collins K (1999) A box H/ACA small nucleolar RNA-like domain at the human telomerase RNA 3′end. Mol Cell Biol 19:567–576

    PubMed  CAS  Google Scholar 

  • Olson MO, Dundr M, Szebeni A (2000) The nucleolus: an old factory with unexpected capabilities. Trends Cell Biol 10:189–196

    Article  PubMed  CAS  Google Scholar 

  • Olson MO, Hingorani K, Szebeni A (2002) Conventional and nonconventional roles of the nucleolus. Int Rev Cytol 219:199–266

    Article  PubMed  CAS  Google Scholar 

  • Pederson T (1998) The plurifunctional nucleolus. Nucleic Acids Res 26:3871–3876

    Article  PubMed  CAS  Google Scholar 

  • Pederson T, Politz JC (2000) The nucleolus and the four ribonucleoproteins of translation. J Cell Biol 148:1091–1095

    Article  PubMed  CAS  Google Scholar 

  • Perry RP (1962) The cellular sites of synthesis of ribosomal and 4S RNA. Proc Natl Acad Sci USA 48:2179–2186

    Article  PubMed  CAS  Google Scholar 

  • Politz JC, Yarovoi KSM, Gowda K, Zwieb C, Pederson T (2000) Signal recognition particle components in the nucleolus. Proc Natl Acad Sci USA 97:55–60

    Article  PubMed  CAS  Google Scholar 

  • Politz JC, Lewandowski LB, Pederson T (2002) Signal recognition particle RNA localization within the nucleolus differs from the classical sites of ribosome synthesis. J Cell Biol 159:411–418

    Article  PubMed  CAS  Google Scholar 

  • Raska I, Shaw PJ, Cmarko D (2006) New insights into nucleolar architecture and activity. Int Rev Cytol 255:177–235

    Article  PubMed  CAS  Google Scholar 

  • Reddy R, Li WY, Henning D, Choi YC, Nohga K, Busch H (1981) Characterization and subcellular localization of 7-8S RNAs of Novikoff hepatoma. J Biol Chem 256:8452–8457

    PubMed  CAS  Google Scholar 

  • Romisch K, Webb J, Lingelbach K, Gausepohl H, Dobberstein B (1990) The 54-kD protein of signal recognition particle contains a methionie-rich RNA binding domain. J Cell Biol 111:1793–1802

    Article  PubMed  CAS  Google Scholar 

  • Rose MA, Weeks KM (2001) Visualizing induced fit in early assembly of the human signal recognition particle. Nat Struct Biol 8:515–520

    Article  PubMed  CAS  Google Scholar 

  • Scheer U, Hock R (1999) Structure and function of the nucleolus. Curr Opin Cell Biol 11:385–390

    Article  PubMed  CAS  Google Scholar 

  • Scoulica E, Krause E, Meese K, Dobberstein B (1987) Disassembly and domain structure of the proteins in the signal-recognition particle. Eur J Biochem 163:519–528

    Article  PubMed  CAS  Google Scholar 

  • Shan SO, Walter P (2005) Co-translational protein targeting by the signal recognition particle. FEBS Lett 579:921–926

    Article  PubMed  CAS  Google Scholar 

  • Shaw PJ, Jordan EG (1995) The nucleolus. Ann Rev Cell Dev Biol 11:93–121

    Google Scholar 

  • Siegel V, Walter P (1985) Elongation arrest is not a prerequisite for secretory protein translocation across the microsomal membrane. J Cell Biol 100:1913–1921

    Article  Google Scholar 

  • Siegel V, Walter P (1986) Removal of the Alu structural domain from signal recognition particle leaves its protein translocation activity intact. Nature 320:81–84

    Article  Google Scholar 

  • Siegel V, Walter P (1988) Binding of the 19-kDa and 68/72-kDa signal recognition particle (SRP) proteins on SRP RNA as determined by protein-RNA “footprinting”. Proc Natl Acad Sci USA 85:1801–1805

    Article  PubMed  CAS  Google Scholar 

  • Sinha KM, Gu J, Chen Y, Reddy R (1998) Adenylation of small RNAs in human cells. J Biol Chem 273:6853–6859

    Article  PubMed  CAS  Google Scholar 

  • Sinha K, Perumal K, Chen Y, Reddy R (1999) Post-translational adenylation of signal recognition particle RNA is carried out by an enzyme different from mRNA poly(A) polymerase. J Biol Chem 274:30826–30831

    Article  PubMed  CAS  Google Scholar 

  • Sommerville J, Brumwell CL, Ritland Politz JC, Pederson T (2005) Signal recognition particle assembly in relation to the function of amplified nucleoli of Xenopus oocytes. J Cell Sci 118:1299–1307

    Article  PubMed  CAS  Google Scholar 

  • Strub K, Walter P (1990) Assembly of the Alu domain of the signal recognition particle (SRP): dimerization of the two protein components is required for efficient binding to SRP RNA. Mol Biol Cell 10:777–784

    CAS  Google Scholar 

  • Strub K, Moss J, Walter P (1991) Binding sites of the 9- and 14-kilodalton heterodimeric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolution. Mol Cell Biol 11:3949–3959

    PubMed  CAS  Google Scholar 

  • Thomas F, Kutay U (2003) Biogenesis and nuclear export of ribosomal subunits in higher eukaryotes depends on the CRM1 export pathway. J Cell Sci 116:2409–2419

    Article  PubMed  CAS  Google Scholar 

  • Trotta C, Lund E, Kahan L, Johnson AW, Dahlberg JE (2003) Coordinated nuclear export of 60S ribosomal subunits and NMD3 in vertebrates. EMBO J 22:2841–2851

    Article  PubMed  CAS  Google Scholar 

  • Ullu E, Weiner AM (1984) Human genes and pseudogenes for the 7SL RNA component of the signal recognition particle. EMBO J 3:3303–3310

    PubMed  CAS  Google Scholar 

  • Ullu E, Murphy S, Melli M (1982) Human 7SL RNA consists of a 140 nucleotide middle-repetitive sequence inserted in an Alu sequence. Cell 29:195–202

    Article  PubMed  CAS  Google Scholar 

  • Walter P, Blobel G (1980) Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum. Proc Natl Acad Sci USA 77:7112–7116

    Article  PubMed  CAS  Google Scholar 

  • Walter P, Blobel G (1982) Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum. Nature 299:691–698

    Article  PubMed  CAS  Google Scholar 

  • Walter P, Blobel G (1983) Disassembly and reconstitution of signal recognition particle. Cell 34:525–533

    Article  PubMed  CAS  Google Scholar 

  • Walter P, Johnson AE (1994) Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane. Annu Rev Cell Biol 10:87–119

    Article  PubMed  CAS  Google Scholar 

  • Wang J, Cao LG, Wang YL, Pederson T (1991) Localization of pre-messenger RNA at discrete nuclear sites. Proc Natl Acad Sci USA 88:7391–7395

    Article  PubMed  CAS  Google Scholar 

  • Warner JR, Soeiro R (1967) Nascent ribosomes from HeLa cells. Proc Natl Acad Sci USA 58:1984–1990

    Article  PubMed  CAS  Google Scholar 

  • Wiedmann M, Kuzchalia TV, Bielka H, Rapoport TA (1987) Direct probing of the interaction between the signal sequence of nascent preprolactin in the signal recognition particle by specific cross-linking. J Cell Biol 104:201–208

    Article  PubMed  CAS  Google Scholar 

  • Yin J, Yang CH, Zwieb C (2001) Assembly of the human signal recognition particle (SRP): overlap of regions required for binding of protein SRP54 and assembly control. RNA 7:1389–1396

    PubMed  CAS  Google Scholar 

  • Yin J, Iakhiaeva E, Menichelli E, Zwieb C (2007) Identification of the RNA binding regions of SRP68/72 and SRP72 by systematic mutagenesis of human SRP RNA. RNA Biol 4:154–159

    Article  PubMed  CAS  Google Scholar 

  • Zieve G, Benecke BJ, Penman S (1977) Synthesis of two classes of small RNA species in vivo and in vitro. Biochemistry 16:4520–4525

    Article  PubMed  CAS  Google Scholar 

  • Zopf D, Bernstein HD, Johnson AE, Walter P (1990) The methionine-rich domain of the 54 kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence. EMBO J 9:4511–4517

    PubMed  CAS  Google Scholar 

  • Zwieb C, Larsen N (1997) The signal recognition particle database (SRPDB). Nucleic Acids Res 25:107–108

    Article  Google Scholar 

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  1. Saccomanno Research Institute, St. Mary’s Hospital & Medical Center, Grand Junction, CO, USA

    Marty R. Jacobson

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  1. Marty R. Jacobson
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Correspondence to Marty R. Jacobson .

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  1. Dept. Biochemistry, University of Mississippi Medical Center, North State St. 2500, Jackson, 39216, Mississippi, USA

    Mark O. J. Olson

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Jacobson, M.R. (2011). Assembly of Signal Recognition Particles in the Nucleolus. In: Olson, M. (eds) The Nucleolus. Protein Reviews, vol 15. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-0514-6_15

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