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Nuclear transport and nuclear pores in yeast

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Molecular Biology of Saccharomyces
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Abstract

The central features of nuclear import have been conserved during evolution. In yeast the nuclear accumulation of proteins follows the same selective and active transport mechanisms known from higher eukaryotes. Yeast nuclear proteins contain nuclear localization sequences (NLS) which are presumably recognized by receptors in the cytoplasm and the nuclear envelope. Subsequent to this recognition step, nuclear proteins are translocated into the nucleus via the nuclear pore complexes. The structure of the yeast nuclear pore complex resembles that of higher eukaryotes. Recently, the first putative components of the yeast nuclear import machinery have been cloned and sequenced. The genetically amenable yeast system allows for an efficient structural and functional analysis of these components. Due to the evolutionary conservation potential insights into the nuclear import mechanisms in yeast can be transferred to higher eukaryotes. Thus, yeast can be considered as a eukaryotic model system to study nuclear transport.

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References

  • Adam SA & Gerace L (1991) Cytosolic proteins that specifically bind nuclear localization signals are receptors for nuclear import. Cell 66: 837–847

    Article  PubMed  CAS  Google Scholar 

  • Akey CW (1989) Interactions and structure of the nuclear pore complex revealed by cryoelectron microscopy. J. Cell Biol. 109: 955–970

    Article  PubMed  CAS  Google Scholar 

  • — (1990) Visualization of transport-related configurations of the nuclear pore transporter. Biophys. J. 58: 341–355

    Article  PubMed  CAS  Google Scholar 

  • Akey CW & Goldfarb DS (1989) Protein import through the nuclear pore complex is a multistep process. J. Cell Biol. 109: 971–982

    Article  PubMed  CAS  Google Scholar 

  • Allen JL & Douglas MG (1989) Organization of the nuclear pore complex in Saccharomyces cerevisiae. J. Ultrastruc. Molec. Struct. Res. 102: 95–108

    Article  CAS  Google Scholar 

  • Amati BB & Gasser SM (1988) Chromosomal ARS and CEN elements bind specifically to the yeast nuclear scaffold. Cell 54: 967–978

    Article  PubMed  CAS  Google Scholar 

  • Aris, JP & Blobel G (1988) Identification and characterization of a yeast nucleolar protein that is similar to a rat liver nucleolar protein. J. Cell Biol. 107: 17–31

    Article  PubMed  CAS  Google Scholar 

  • — (1989) Yeast nuclear envelope proteins cross-react with an antibody against mammalian pore complex proteins. J. Cell Biol. 108: 2059–2067

    Article  PubMed  CAS  Google Scholar 

  • Bäuerele PA & Baltimore D (1988) ΙxΒ: A specific inhibitor of NF-xΒ transription factor. Science 242: 540–546

    Google Scholar 

  • Barnes G & Rine J (1985) Regulated expression of endonu-clease EcoRI in Saccharomyces cerevisiae: nuclear entry and biological consequences. Proc. Natl. Acad. Sci. USA. 82: 1354–1358

    Article  PubMed  CAS  Google Scholar 

  • Bataillé Ν, Heiser Τ & Fried HM (1990) Cytoplasmic transport of ribosomal subunits microinjeeted into the Xenopus laevis

    Google Scholar 

  • oocyte nucleus: a generalized, facilitated process. J. Cell Biol. 111: 1571–1582

    Google Scholar 

  • Breeuwer Μ & Goldfarb Μ (1990) Facilitated nuclear transport of histone H1 and other small nucleophilic proteins. Cell 60: 999–1008

    Article  PubMed  CAS  Google Scholar 

  • Cardenas ME, Laroche Τ & Gasser SM (1990) The composition and morphology of yeast nuclear scaffolds. J. Cell Sci. 96: 439–450

    PubMed  CAS  Google Scholar 

  • Carmo-Fonseca M, Cidadao AJ & David-Ferreira JF (1987) Filamentous cross-bridges link intermediate filaments to the nuclear pore complexes. Eur. J. Cell Biol. 45: 282–290

    Google Scholar 

  • Carmo-Fonseca Μ, Kern Η & Hurt EC (1991) Human nucleo-porin p62 and the essential yeast nuclear pore protein NSP1 show sequence homology and a similar domain organization. Eur. J. Cell Biol. 55: 17–30

    Google Scholar 

  • Cohen C & Parry DAD (1990) α-helical coiled coils and bundles: how to design an α-helical protein. Proteins 7: 1–15

    Google Scholar 

  • Cordes V, Waizenegger I & Krohne G (1991) Nuclear pore complex glycoprotein p62 of Xenopus laevis and mouse: cDNA cloning and identification of its glycosylated region. Eur. J. Cell Biol. 55: 31–47

    Google Scholar 

  • Dabauvalle MC, Schulz Β, Scheer U & Peters R (1988) Inhibition of nuclear accumulation of karyophilic proteins in living cells by microinjection of the lectin wheat germ agglutinin. Exp. Cell Res. 174: 291–296

    Google Scholar 

  • Dabauvalle M-C, Loos Κ & Scheer U (1990) Identification of a soluble precursor complex essential for nuclear pore assembly. Chromosoma 100: 56–66

    Article  PubMed  CAS  Google Scholar 

  • Davis LI & Blobel (1986) Identification and characterization of a nuclear pore complex protein. Cell 45: 699–709

    Article  PubMed  CAS  Google Scholar 

  • — (1987) Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway. Proc. Natl. Acad. Sci. USA 84: 7552–7556

    Article  PubMed  CAS  Google Scholar 

  • Davis LI & Fink GR (1990) The NUP1 gene encodes an essential component of the yeast nuclear pore complex. Cell 61: 965–978

    Article  PubMed  CAS  Google Scholar 

  • Dingwall C, Sharnick SV & Laskey RA (1982) A polypeptide domain that specifies migration of nucleoplasmin into the nucleus. Cell 30: 449–458

    Article  PubMed  CAS  Google Scholar 

  • Featherstone C, Darby MK & Gerace L (1988) A monoclonal antibody against the nuclear pore complex inhibits nucleocy-toplasmic transport of protein and RNA in-vivo. J. Cell Biol. 107: 1289–1297

    Article  PubMed  CAS  Google Scholar 

  • Feldherr CM, Kallenbach Ε & Schultz Ν (1984) Movement of a karyophilic protein through the nuclear pores of oocytes. J. Cell Biol. 99: 2216–2222

    Article  PubMed  CAS  Google Scholar 

  • Finlay DR & Forbes DJ (1990) Reconstitution of biochemically altered nuclear pores: transport can be eliminated and restored. Cell 60: 17–29

    Article  PubMed  CAS  Google Scholar 

  • Finlay DR, Newmeyer DD, Price TM & Forbes DJ (1987) Inhibition of in-vitro nuclear transport by a lectin that binds to nuclear pores. J. Cell Biol. 104: 189–200

    Article  PubMed  CAS  Google Scholar 

  • Finlay DR, Meier E, Bradley P, Horecka J & Forbes DJ (1991) A complex of nuclear pore proteins required for pore functions. J. Cell Biol. 114: 169–183

    Article  PubMed  CAS  Google Scholar 

  • Franke WW (1974) Structure, biochemistry and functions of the nuclear envelope. Int. Rev. Cytol. 4: 72–236

    Google Scholar 

  • Garcia-Bustos JF, Wagner Ρ & Hall MN (1991) Yeast cell-free nuclear protein import requires ATP hydrolysis. Exp. Cell Res. 192: 213–219

    Google Scholar 

  • Georgatos SD, Maroulakou I & Blobel G (1989) Lamin A, Lamin B, and Lamin Β receptor analogues in yeast. J. Cell Biol. 108: 2069–2082

    Google Scholar 

  • Goldfarb D (1988) Karyophilic peptides: applications to the study of nuclear transport. Cell Biol. Inter. Reports. 12: 809–832

    Article  CAS  Google Scholar 

  • Ghosh S & Baltimore D (1990) Activation in vitro of NF-xΒ by phosphorylation of its inhibitor ΙxΒ. Nature 344: 678–682

    Article  PubMed  CAS  Google Scholar 

  • Greber UF, Senior A & Gerace L (1990) A major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large luminal domain and a small cytoplasmic tail. EMBOJ. 9: 1495–1502

    CAS  Google Scholar 

  • Hall MN, Hereford L & Herskowitz I (1984) Targeting of E. coli b-galactosidase to the nucleus in yeast. Cell 36: 1057–1065

    Article  PubMed  CAS  Google Scholar 

  • Hall MN, Craik C & Hiraoka Υ (1990) Homeodomain of yeast repressor alpha 2 contains a nuclear localization signal. Proc. Natl. Acad. Sci. USA 87: 6954–6958

    Google Scholar 

  • Hart GW, Haltiwanger RS, Holt GD & Kelly WG (1989) Glycosylation in the nucleus and cytoplasm. Ann. Rev. Biochem. 58: 841–874

    Google Scholar 

  • Hurt EC (1988) A novel nucleoskeletal-like protein located at the nuclear periphery is required for the life cycle of Saccharo-myces cerevisiae. EMBO J. 7: 4323–4334

    PubMed  CAS  Google Scholar 

  • — (1989) NSPl, a yeast protein located at the nuclear periphery, is required for the cell cycle of Saccharomyces cerevisiae. J. Cell Sci. 12: 243–252

    CAS  Google Scholar 

  • — (1990) Targeting of a cytosolic protein to the nuclear periphery. J. Cell Biol. 111: 2829–2837

    Article  PubMed  CAS  Google Scholar 

  • Hurt EC, McDowall A & Schimmang Τ (1988) Nucleolar and nuclear envelope proteins of the yeast Saccharomyces cerevisiae. Eur. J. Cell Biol. 46: 554–563

    Google Scholar 

  • Hurt EC, McDowall A & Schimmang Τ (1988) Nucleolar and nuclear envelope proteins of the yeast Saccharomyces cerevisiae. Eur. J. Cell Biol. 46: 554–563

    Google Scholar 

  • Jordan EG, Severs NJ & Williamson DH (1977) Nuclear pore formation and the cell cycle in Saccharomyces cerevisiae. Exp. Cell Res. 104: 446–449

    Google Scholar 

  • Kalderon D, Roberts BL, Richardson WP & Smith AE (1984) A short amino acid sequence able to specify nuclear location. Cell 39: 499–509

    Article  PubMed  CAS  Google Scholar 

  • Kalinich J F & Douglas MG (1989) In vitro translocation through the yeast nuclear envelope. J. Biol. Chem. 264: 17979–17989

    Google Scholar 

  • Lee WC & Melese Τ (1989) Identificaton and characterization of a nuclear localization sequence-binding protein in yeast. Proc. Natl. Acad. Sci. USA 86: 8808–8812

    Article  PubMed  CAS  Google Scholar 

  • Lee WC, Xue Ζ & Melese Τ (1991) The NSRI gene encodes a protein that specifically binds nuclear localization sequences and has two RNA recognition motifs. J. Cell Biol. 113: 1–12

    Article  PubMed  CAS  Google Scholar 

  • Mann Κ & Mecke D (1980) Isolation and characterization of nuclei and nuclear membranes from Saccharomyces cerevisiae protoplasts. FEBS Lett. 122: 95–99

    Article  PubMed  CAS  Google Scholar 

  • Mann K-H & Mecke D (1982) The isolation of Saccharomyces cerevisiae nuclear membranes with nuclease and high-salt treatment. Biochim. Biophys. Acta 687: 57–62

    Article  PubMed  CAS  Google Scholar 

  • Maul GG (1977) The nuclear and cytoplasmic pore complex: structure, dynamics, distribution and evolution. Int. Rev. Cytol. 6: 75–186

    CAS  Google Scholar 

  • Meier UT & Blobel G (1990) A nuclear localization signal binding protein in the nucleolus. J. Cell Biol. 111: 2235–2245

    Article  PubMed  CAS  Google Scholar 

  • MoII T, Tebb G, Surana U, Robitsch Η & Nasmyth Κ (1991) The role of phosphorylation and the CDC28 protein kinase in cell-cycle regulated nuclear import of the S. cerevisiae transcription factor SWI5. Cell 66: 743–758

    Article  Google Scholar 

  • Moor Η & Mühlethaler Κ (1963) Fine structure in frozen-etched yeast cells. J. Cell Biol. 17: 609–627

    Article  PubMed  CAS  Google Scholar 

  • Moreland RB, Nam HG, Hereford LM & Fried HM (1985) Identification of a nuclear localization signal of a yeast riboso-mal protein. Proc. Natl. Acad. Sci. USA 82: 6561–6565

    Google Scholar 

  • Moreland RB, Langevin GL, Singer RH, Garcea RL & Hereford LM (1987) Amino acid sequences that determine the nuclear localization of yeast histone 2B. Mol. Cell Biol. 7: 4048–4057

    Google Scholar 

  • Nasmyth K, Seddon A & Ammerer G (1987) Cell cycle regulation of SW15 is required for mother-cell-specific HO transcription in yeast. Cell 49: 549–558

    Article  PubMed  CAS  Google Scholar 

  • Nasmyth K, Adolf G, Lydall D & Seddon A (1990) The identification of a second cell cycle control on the HO promoter in yeast: cell cycle regulation of SWI5 nuclear entry. Cell 62: 631–647

    Article  PubMed  CAS  Google Scholar 

  • Nehrbass U, Kern H, Mutvei A, Horstmann Η, Marshallsay Β & Hurt EC (1990) NSPl: A yeast nuclear envelope protein localized at the nuclear pores exerts its essential function by its carboxy-terminal domain. Cell 61: 979–989

    Google Scholar 

  • Nelson Μ & Silver Ρ (1989) Context affects nuclear protein localization in Saccharomyces cerevisiae. Mol. Cell Biol. 9: 384–389

    PubMed  CAS  Google Scholar 

  • Newmeyer DD & Forbes DJ (1988) Nuclear import can be separated into distinct steps in vitro: nuclear pore binding and translocation. Cell 52: 641–653

    Article  PubMed  CAS  Google Scholar 

  • Park MK, D’Onofrio M, Willingham MC & Hanover JA (1987) A monoclonal antibody against a family of nuclear pore proteins (nucleoporins): O-linked N-acetylglucosamine is part of the immunodeterminant. Proc. Natl. Acad. Sci. USA 84: 6462–6466

    Google Scholar 

  • Peters R (1986) Fluorescence microphotolysis to measure nucle-ocytoplasmic transport and intracellular mobility. Biochim. Biophys. Acta 864: 305–359

    Article  PubMed  CAS  Google Scholar 

  • Picard D & Yamamoto KR (1987) Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor. EMBO J. 6: 3333–3340

    PubMed  CAS  Google Scholar 

  • Richardson WD, Mills AD, Dilworth SM, Laskey RA & Dingwall C (1988) Nuclear protein migration involves two steps: rapid binding at the nuclear envelope followed by slower translocation through nuclear pores. Cell 52: 655–664

    Article  PubMed  CAS  Google Scholar 

  • Rihs H-P & Peters R (1989) Nuclear transport kinetics depend on phosphorylation site-containing sequences flanking the karyophilic signal of the SV40 T-antigen. EMBO J. 8: 1479–1484

    PubMed  CAS  Google Scholar 

  • Rihs H-P, Jans DA, Fan Η & Peters R (1991) The rate of nuclear cytoplasmic protein transport is determined by the casein kinase II site flanking the nuclear localization sequence of the SV40 T-antigen. EMBO J. 10: 633–639

    PubMed  CAS  Google Scholar 

  • Robbins J, Dilworth SM, Laskey RA & Dingwall C (1991) Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence. Cell 64: 615–623

    Google Scholar 

  • Roberts BL, Richardson WD & Smith AE (1987) The effect of protein context on nuclear location signal function. Cell 50: 465–475

    Article  PubMed  CAS  Google Scholar 

  • Rothblatt JA, Deshaies SL, Sanders SL, Daum G & Schekman R (1989) Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast. J. Cell Biol. 109: 2641–2652

    Article  PubMed  CAS  Google Scholar 

  • Sadler I, Chiang A, Kurihara T, Rothblatt J, Way J & Silver Ρ (1989) A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein. J. Cell Biol. 109: 2665–2675

    Article  PubMed  CAS  Google Scholar 

  • Sanchez ER, Schlesinger MJ & Pratt WB (1985) The 90 kD non-steroid-binding phosphoprotein that binds to the un-transformed glucocorticoid receptor in molybdate stabilized L-cell cytosol is the murine 90 kD heat shock protein. J. Biol. Chem. 260: 12398–12401

    Google Scholar 

  • Silver P, Sadler I & Osborne MA (1989) Yeast proteins that recognize nuclear localization sequences. J. Cell Biol. 109: 983–989

    Article  PubMed  CAS  Google Scholar 

  • Silver PA, Keegan LP & Ptashne Μ (1984) Amino terminus of the yeast GAL4 gene product is sufficient for nuclear localization. Proc. Natl. Acad. Sci. USA 81: 5951–5955

    Google Scholar 

  • Snow CM, Senior A & Gerace L (1987) Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J. Cell Biol. 104: 1143–1156

    Article  PubMed  CAS  Google Scholar 

  • Starr CM & Hanover JA (1991) A common structural motif in nuclear pore proteins (nucleoporins). BioEssays 13: 145–146

    Article  PubMed  CAS  Google Scholar 

  • Steinert PM & Roop DR (1988) Molecular and cellular biology of intermediate filaments. Ann. Rev. Biochem. 57: 593–625

    Article  PubMed  CAS  Google Scholar 

  • Steinert PM, Steven AC & Roop DR (1985) The molecular biology of intermediate filaments. Cell 42: 411–419

    Article  PubMed  CAS  Google Scholar 

  • Stochaj U, Osborne Μ, Kurihara Τ & Silver Ρ (1991) A yeast protein that binds nuclear localization signals: Purification, localization, and antibody inhibition of binding activity. J. Cell Biol. 113: 1243–1254

    Google Scholar 

  • Underwood MR & Fried HM (1990) Characterization of nuclear localization sequences derived from the yeast ribosomal protein L29. EMBO J. 9: 91–99

    PubMed  CAS  Google Scholar 

  • Wozniak RK, Bartnik Ε & Blobel G (1989) Primary structure analysis of an integral membrane glycoprotein of the nuclear pore. J. Cell Biol. 108: 2083–2092

    Article  PubMed  CAS  Google Scholar 

  • Yoneda Y, Imamoto-Sonobe N, Yamaizumi Μ & Uchida Τ (1987) Reversible inhibition of protein import into the nucleus by wheat germ agglutinin injected into cultured cells. Exp. Cell Res. 173: 586–595

    Google Scholar 

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© 1992 Springer Science+Business Media Dordrecht

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Nehrbass, U., Hurt, E.C. (1992). Nuclear transport and nuclear pores in yeast. In: Grivell, L.A. (eds) Molecular Biology of Saccharomyces . Springer, Dordrecht. https://doi.org/10.1007/978-94-011-2504-8_1

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  • DOI: https://doi.org/10.1007/978-94-011-2504-8_1

  • Publisher Name: Springer, Dordrecht

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