Comprehensive analysis of diverse ribonucleoprotein complexes (original) (raw)

• Rigaut, G. et al. A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17, 1030–1032 (1999).
  Article CAS Google Scholar
• Saveanu, C. et al. Nog2p, a putative GTPase associated with pre-60S subunits and required for late 60S maturation steps. EMBO J. 20, 6475–6484 (2001).
  Article CAS Google Scholar
• Gavin, A.C. et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415, 141–147 (2002).
  Article CAS Google Scholar
• Ho, Y. et al. Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry. Nature 415, 180–183 (2002).
  Article CAS Google Scholar
• Sorger, P.K., Ammerer, G. & Shore, D. in Protein Function: a Practical Approach. (ed. Creighton, T.) 199–278 (IRL Press, Oxford, 1989).
  Google Scholar
• Lewis, J.D., Goerlich, D. & Mattaj, I. A yeast cap binding protein complex (yCBC) acts at an early step in pre-mRNA splicing. Nucl. Acids Res. 24, 3332–3336 (1996).
  Article CAS Google Scholar
• Gavin, A.C. et al. Proteome survey reveals modularity of the yeast cell machinery. Nature 440, 631–636 (2006).
  Article CAS Google Scholar
• Oeffinger, M. & Tollervey, D. Yeast Nop15p is an RNA-binding protein required for pre-rRNA processing and cytokinesis. EMBO J. 22, 6573–6583 (2003).
  Article CAS Google Scholar
• Segref, A. et al. Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear pores. EMBO J. 16, 3256–3271 (1997).
  Article CAS Google Scholar
• Harnpicharnchai, P. et al. Composition and functional characterization of yeast 66s ribosome assembly intermediates. Mol. Cell 8, 505–515 (2001).
  Article CAS Google Scholar
• Schafer, T., Strauss, D., Petfalski, E., Tollervey, D. & Hurt, E. The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes. EMBO J. 22, 1370–1380 (2003).
  Article Google Scholar
• Henry, Y. et al. The 5′ end of yeast 5.8S rRNA is generated by exonucleases from an upstream cleavage site. EMBO J. 13, 2452–2463 (1994).
  Article CAS Google Scholar
• Krogan, N.J. et al. Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440, 637–643 (2006).
  Article CAS Google Scholar
• Burckstummer, T. et al. An efficient tandem affinity purification procedure for interaction proteomics in mammalian cells. Nat. Methods 3, 1013–1019 (2006).
  Article Google Scholar
• Hurt, E. et al. Mex67p mediates nuclear export of a variety of RNA polymerase II transcripts. J. Biol. Chem. 275, 8361–8368 (2000).
  Article CAS Google Scholar
• Warner, J.R. The assembly of ribosomes in yeast. J. Biol. Chem. 246, 447–454 (1971).
  CAS PubMed Google Scholar
• Stewart, M. Ratcheting mRNA out of the nucleus. Mol. Cell 25, 327–330 (2007).
  Article CAS Google Scholar
• Arava, Y. et al. Genome-wide analysis of mRNA translation profiles in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 100, 3889–3894 (2003).
  Article CAS Google Scholar
• Vinciguerra, P. & Stutz, F. mRNA export: an assembly line from genes to nuclear pores. Curr. Opin. Cell Biol. 16, 285–292 (2004).
  Article CAS Google Scholar
• Jimeno, S., Rondon, A.G., Luna, R. & Aguilera, A. The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability. EMBO J. 21, 3526–3535 (2002).
  Article CAS Google Scholar
• Strasser, K. & Hurt, E. Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA export. EMBO J. 19, 410–420 (2000).
  Article CAS Google Scholar
• Zenklusen, D., Vinciguerra, P., Strahm, Y. & Stutz, F. The yeast hnRNP-Like proteins Yra1p and Yra2p participate in mRNA export through interaction with Mex67p. Mol. Cell. Biol. 21, 4219–4232 (2001).
  Article CAS Google Scholar
• Vinciguerra, P., Iglesias, N., Camblong, J., Zenklusen, D. & Stutz, F. Perinuclear Mlp proteins downregulate gene expression in response to a defect in mRNA export. EMBO J. 24, 813–823 (2005).
  Article CAS Google Scholar
• Andrulis, E.D. et al. Esc1, a nuclear periphery protein required for Sir4-based plasmid anchoring and partitioning. Mol. Cell. Biol. 22, 8292–8301 (2002).
  Article CAS Google Scholar
• Duncan, K., Umen, J.G. & Guthrie, C. A putative ubiquitin ligase required for efficient mRNA export differentially affects hnRNP transport. Curr. Biol. 10, 687–696 (2000).
  Article CAS Google Scholar
• Lei, E.P. et al. Sac3 is an mRNA export factor that localizes to cytoplasmic fibrils of nuclear pore complex. Mol. Biol. Cell 14, 836–847 (2003).
  Article CAS Google Scholar
• Ghaemmaghami, S. et al. Global analysis of protein expression in yeast. Nature 425, 737–741 (2003).
  Article CAS Google Scholar
• Long, R.M. et al. Mating type switching in yeast controlled by asymmetric localization of ASH1 mRNA. Science 277, 383–387 (1997).
  Article CAS Google Scholar
• Takizawa, P.A. & Vale, R.D. The myosin motor, Myo4p, binds Ash1 mRNA via the adapter protein, She3p. Proc. Natl. Acad. Sci. USA 97, 5273–5278 (2000).
  Article CAS Google Scholar
• Shepard, K.A. et al. Widespread cytoplasmic mRNA transport in yeast: identification of 22 bud-localized transcripts using DNA microarray analysis. Proc. Natl. Acad. Sci. USA 100, 11429–11434 (2003).
  Article CAS Google Scholar
• Reck-Peterson, S.L., Tyska, M.J., Novick, P.J. & Mooseker, M.S. The yeast class V myosins, Myo2p and Myo4p, are nonprocessive actin-based motors. J. Cell Biol. 153, 1121–1126 (2001).
  Article CAS Google Scholar
• Pruyne, D. & Bretscher, A. Polarization of cell growth in yeast. J. Cell Sci. 113, 571–585 (2000).
  CAS PubMed Google Scholar
• Rout, M.P. et al. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148, 635–651 (2000).
  Article CAS Google Scholar