RNA-quality control by the exosome (original) (raw)

• Warner, J. R. The economics of ribosome biosynthesis in yeast. Trends Biochem. Sci. 24, 437?440 (1999).
  Article CAS PubMed Google Scholar
• Parker, R. & Song, H. The enzymes and control of eukaryotic mRNA turnover. Nature Struct. Mol. Biol. 11, 121?127 (2004).
  Article CAS Google Scholar
• Mitchell, P., Petfalski, E., Shevchenko, A., Mann, M. & Tollervey, D. The exosome; a conserved eukaryotic RNA processing complex containing multiple 3′→5′ exoribonuclease activities. Cell 91, 457?466 (1997).
  Article CAS PubMed Google Scholar
• Allmang, C. et al. The yeast exosome and human PM-Scl are related complexes of 3′→5′ exonucleases. Genes Dev. 13, 2148?2158 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Peng, W. T. et al. A panoramic view of yeast noncoding RNA processing. Cell 113, 919?933 (2003).
  Article CAS PubMed Google Scholar
• Burkard, K. T. & Butler, J. S. A nuclear 3′?5′ exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3p. Mol. Cell. Biol. 20, 604?616 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Araki, Y. et al. Ski7p G protein interacts with the exosome and the Ski complex for 3′-to-5′ mRNA decay in yeast. EMBO J. 20, 4684?4693 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• van Hoof, A., Staples, R. R., Baker, R. E. & Parker, R. Function of the ski4p (Csl4p) and Ski7p proteins in 3′-to-5′ degradation of mRNA. Mol. Cell. Biol. 20, 8230?8243 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Mitchell, P. et al. Rrp47p is an exosome-associated protein required for the 3′ processing of stable RNAs. Mol. Cell. Biol. 23, 6982?6992 (2003).
  Article CAS PubMed PubMed Central Google Scholar
• Yavuzer, U., Smith, G. C., Bliss, T., Werner, D. & Jackson, S. P. DNA end-independent activation of DNA-PK mediated via association with the DNA-binding protein C1D. Genes Dev. 12, 2188?2199 (1998).
  Article CAS PubMed PubMed Central Google Scholar
• van Hoof, A., Lennertz, P. & Parker, R. Yeast exosome mutants accumulate 3′-extended polyadenylated forms of U4 small nuclear RNA and small nucleolar RNAs. Mol. Cell. Biol. 20, 441?452 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Zanchin, N. I. & Goldfarb, D. S. The exosome subunit Rrp43p is required for the efficient maturation of 5.8S, 18S and 25S rRNA. Nucleic Acids Res. 27, 1283?1288 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Allmang, C. et al. Functions of the exosome in rRNA, snoRNA and snRNA synthesis. EMBO J. 18, 5399?5410 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• de la Cruz, J., Kressler, D., Tollervey, D. & Linder, P. Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for the 3′ end formation of 5.8S rRNA in Saccharomyces cerevisiae. EMBO J. 17, 1128?1140 (1998).
  Article CAS PubMed PubMed Central Google Scholar
• Grosshans, H., Deinert, K., Hurt, E. & Simos, G. 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 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Allmang, C., Mitchell, P., Petfalski, E. & Tollervey, D. Degradation of ribosomal RNA precursors by the exosome. Nucleic Acids Res. 28, 1684?1691 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Wyers, F. et al. Cryptic Pol II transcripts are degraded by a nuclear quality control pathway involving a new poly(A) polymerase. Cell 121, 725?737 (2005). Shows that the TRAMP complex and the exosome rapidly degrade transcripts that are produced from intergenic regions. These transcripts are very common, being produced from up to 10% of intergenic regions under normal conditions.
  Article CAS PubMed Google Scholar
• LaCava, J. et al. RNA degradation by the exosome is promoted by a nuclear polyadenylation complex. Cell 21, 713?724 (2005).
  Article CAS Google Scholar
• Vanacova, S. et al. A new yeast poly(A) polymerase complex involved in RNA quality control. PLoS Biol. 3, e189 (2005). A biochemical analysis of the activity of the TRAMP complex, showing that it can recruit the exosome to degrade an aberrant tRNA in vitro.
  Article PubMed CAS Google Scholar
• Kadaba, S. et al. Nuclear surveillance and degradation of hypomodified initiator tRNAMet in S. cerevisiae. Genes Dev. 18, 1227?1240 (2004). First report that polyadenylation by Trf4 is linked to RNA degradation by the exosome.
  Article CAS PubMed PubMed Central Google Scholar
• Torchet, C. et al. Processing of 3′ extended read-through transcripts by the exosome can generate functional mRNAs. Mol. Cell 9, 1285?1296 (2002).
  Article CAS PubMed Google Scholar
• Hilleren, P., McCarthy, T., Rosbash, M., Parker, R. & Jensen, T. H. Quality control of mRNA 3′-end processing is linked to the nuclear exosome. Nature 413, 538?542 (2001).
  Article CAS PubMed Google Scholar
• Bousquet-Antonelli, C., Presutti, C. & Tollervey, D. Identification of a regulated pathway for nuclear pre-mRNA turnover. Cell 102, 765?775 (2000).
  Article CAS PubMed Google Scholar
• Lee, A., Henras, A. K. & Chanfreau, G. Multiple RNA surveillance pathways limit aberrant expression of iron uptake mRNAs and prevent iron toxicity in S. cerevisiae. Mol. Cell 19, 39?51 (2005). Reports that mRNA-encoding proteins that are involved in iron metabolism are subject to various different nuclear RNA-surveillance pathways.
  Article CAS PubMed Google Scholar
• Kuai, L., Das, B. & Sherman, F. A nuclear degradation pathway controls the abundance of normal mRNAs in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 102, 13962?13967 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Roth, K. M., Wolf, M. K., Rossi, M. & Butler, J. S. The nuclear exosome contributes to autogenous control of NAB2 mRNA levels. Mol. Cell. Biol. 25, 1577?1585 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Houalla, R. et al. Microarray detection of novel nuclear RNA substrates for the exosome. Yeast 23, 439?454 (2006).
  Article CAS PubMed Google Scholar
• Anderson, J. S. J. & Parker, R. P. The 3′ to 5′ degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3′ to 5′ exonucleases of the exosome complex. EMBO J. 17, 1497?1506 (1998).
  Article CAS PubMed PubMed Central Google Scholar
• Takahashi, S., Araki, Y., Sakuno, T. & Katada, T. Interaction between Ski7p and Upf1p is required for nonsense-mediated 3′-to-5′ mRNA decay in yeast. EMBO J. 22, 3951?3959 (2003).
  Article CAS PubMed PubMed Central Google Scholar
• Mitchell, P. & Tollervey, D. An NMD pathway in yeast involving accelerated deadenylation and exosome-mediated 3′→5′ degradation. Mol. Cell 11, 1405?1413 (2003).
  Article CAS PubMed Google Scholar
• Lejeune, F., Li, X. & Maquat, L. E. Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities. Mol. Cell 12, 675?687 (2003).
  Article CAS PubMed Google Scholar
• Frischmeyer, P. A. et al. An mRNA surveillance mechanism that eliminates transcripts lacking termination codons. Science 295, 2258?2261 (2002).
  Article CAS PubMed Google Scholar
• van Hoof, A., Frischmeyer, P. A., Dietz, H. C. & Parker, R. Exosome-mediated recognition and degradation of mRNAs lacking a termination codon. Science 295, 2262?2264 (2002).
  Article CAS PubMed Google Scholar
• Tran, H., Schilling, M., Wirbelauer, C., Hess, D. & Nagamine, Y. Facilitation of mRNA deadenylation and decay by the exosome-bound, DExH protein RHAU. Mol. Cell 13, 101?111 (2004).
  Article CAS PubMed Google Scholar
• Chen, C. Y. et al. AU binding proteins recruit the exosome to degrade ARE-containing mRNAs. Cell 107, 451?464 (2001).
  Article CAS PubMed Google Scholar
• Mukherjee, D. et al. The mammalian exosome mediates the efficient degradation of mRNAs that contain AU-rich elements. EMBO J. 21, 165?174 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Gherzi, R. et al. A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery. Mol. Cell 14, 571?583 (2004).
  Article CAS PubMed Google Scholar
• Doma, M. K. & Parker, R. Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation elongation. Nature 440, 561?564 (2006). First report of a yeast mRNA-surveillance pathway that is initiated by RNA cleavage.
  Article CAS PubMed PubMed Central Google Scholar
• Tollervey, D. RNA lost in translation. Nature 440, 425?426 (2006).
  Article CAS PubMed Google Scholar
• Orban, T. I. & Izaurralde, E. Decay of mRNAs targeted by RISC requires XRN1, the Ski complex, and the exosome. RNA 11, 459?469 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Symmons, M. F., Jones, G. H. & Luisi, B. F. A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation. Struct. Fold. Des. 8, 1215?1226 (2000).
  Article CAS Google Scholar
• Stickney, L. M., Hankins, J. S., Miao, X. & Mackie, G. A. Function of the conserved S1 and KH domains in polynucleotide phosphorylase. J. Bacteriol. 187, 7214?7121 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Valentine, R. C., Thang, M. N. & Grunberg-Manago, M. Electron microscopy of Escherichia coli polynucleotide phosphorylase molecules and polyribonucleotide formation. J. Mol. Biol. 39, 389?391 (1969).
  Article CAS PubMed Google Scholar
• Spickler, C. & Mackie, G. A. Action of RNase II and polynucleotide phosphorylase against RNAs containing stem-loops of defined structure. J. Bacteriol. 182, 2422?2427 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Lorentzen, E. et al. The archaeal exosome core is a hexameric ring structure with three catalytic subunits. Nature Struct. Mol. Biol. 12, 575?581 (2005). The first structure of the archaeal exosome, which showed that only one of the archaeal RNase PH-like exosome subunits is an active ribonuclease, although both are required for activity.
  Article CAS Google Scholar
• Lorentzen, E. & Conti, E. Structural basis of 3′ end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core. Mol. Cell 20, 473?481 (2005). Following from the previous analysis, the authors show here how the exosome binds and degrades substrate RNAs.
  Article CAS PubMed Google Scholar
• Buttner, K., Wenig, K. & Hopfner, K. P. Structural framework for the mechanism of archaeal exosomes in RNA processing. Mol. Cell 20, 461?471 (2005). This work characterizes the structure of the complete archaeal exosome.
  Article PubMed CAS Google Scholar
• Symmons, M. F., Williams, M. G., Luisi, B. F., Jones, G. H. & Carpousis, A. J. Running rings around RNA: a superfamily of phosphate-dependent RNases. Trends Biochem. Sci. 27, 11?18 (2002).
  Article CAS PubMed Google Scholar
• Aloy, P. et al. A complex prediction: three-dimensional model of the yeast exosome. EMBO Rep. 3, 628?635 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• van Hoof, A. & Parker, R. The exosome: a proteasome for RNA? Cell 99, 347?350 (1999).
  Article CAS PubMed Google Scholar
• Andrulis, E. D. et al. The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila. Nature 420, 837?841 (2002).
  Article CAS PubMed Google Scholar
• Brouwer, R., Pruijn, G. J. & van Venrooij, W. J. The human exosome: an autoantigenic complex of exoribonucleases in myositis and scleroderma. Arthritis Res. 3, 102?106 (2001).
  Article CAS PubMed Google Scholar
• Brouwer, R. et al. Three novel components of the human exosome. J. Biol. Chem. 276, 6177?6184 (2001).
  Article CAS PubMed Google Scholar
• Estevez, A. M., Kempf, T. & Clayton, C. The exosome of Trypanosoma brucei. EMBO J. 20, 3831?3839 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Chekanova, J. A., Dutko, J. A., Mian, I. S. & Belostotsky, D. A. Arabidopsis thaliana exosome subunit AtRrp4p is a hydrolytic 3′→5′ exonuclease containing S1 and KH RNA-binding domains. Nucleic Acids Res. 30, 695?700 (2002).
  Article CAS PubMed PubMed Central Google Scholar
• Briggs, M. W., Burkard, K. T. & Butler, J. S. Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is essential for efficient 5.8 S rRNA 3′ end formation. J. Biol. Chem. 273, 13255?13263 (1998).
  Article CAS PubMed Google Scholar
• Phillips, S. & Butler, J. S. Contribution of domain structure to the RNA 3′ end processing and degradation functions of the nuclear exosome subunit Rrp6p. RNA 9, 1098?1107 (2003).
  Article CAS PubMed PubMed Central Google Scholar
• Raijmakers, R., Egberts, W. V., van Venrooij, W. J. & Pruijn, G. J. Protein?protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring. J. Mol. Biol. 323, 653?663 (2002).
  Article CAS PubMed Google Scholar
• Estevez, A. M., Lehner, B., Sanderson, C. M., Ruppert, T. & Clayton, C. The roles of intersubunit interactions in exosome stability. J. Biol. Chem. 278, 34943?34951 (2003).
  Article CAS PubMed Google Scholar
• Lehner, B. & Sanderson, C. M. A protein interaction framework for human mRNA degradation. Genome Res. 14, 1315?1323 (2004).
  Article CAS PubMed PubMed Central Google Scholar
• Milligan, L., Torchet, C., Allmang, C., Shipman, T. & Tollervey, D. A nuclear surveillance pathway for mRNAs with defective polyadenylation. Mol. Cell. Biol. 25, 9996?10004 (2005). Describes how the exosome responds to mRNA molecules with defective poly(A) tails.
  Article CAS PubMed PubMed Central Google Scholar
• Wang, L., Lewis, M. S. & Johnson, A. W. Domain interactions within the Ski2?3?8 complex and between the Ski complex and Ski7p. RNA 11, 1291?1302 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Arigo, J. T., Carroll, K. L., Ames, J. M. & Corden, J. L. Regulation of yeast NRD1 expression by premature transcription termination. Mol. Cell 21, 641?651 (2006). Reports that autoregulation of Nrd1 expression involves the RNA-binding proteins Nrd1 and Nab3 as well as the exosome.
  Article CAS PubMed Google Scholar
• Vasiljeva, L. & Buratowski, S. Nrd1 Interacts with the nuclear exosome for 3′ processing of RNA polymerase II transcripts. Mol. Cell 21, 239?248 (2006). Reports a second exosome-stimulating complex. The Nrd1 protein binds to a specific target-RNA sequence and recruits the exosome to facilitate degradation.
  Article CAS PubMed 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).
  Article CAS PubMed PubMed 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. Nature 413, 327?331 (2001).
  Article CAS PubMed Google Scholar
• Puig, S., Askeland, E. & Thiele, D. J. Coordinated remodeling of cellular metabolism during iron deficiency through targeted mRNA degradation. Cell 120, 99?110 (2005). Reports that an ARE-mediated mRNA-degradation system functions in yeast and involves the yeast homologue of the well characterized human ARE-binding protein TTP.
  Article CAS PubMed Google Scholar
• Houseley, J. & Tollervey, D. Yeast Trf5p is a nuclear poly(A) polymerase. EMBO Rep. 7, 205?211 (2005).
  Article PubMed Central CAS Google Scholar
• Egecioglu, D. E., Henras, A. K. & Chanfreau, G. F. Contributions of Trf4p- and Trf5p-dependent polyadenylation to the processing and degradative functions of the yeast nuclear exosome. RNA 12, 26?32 (2006). References 68 and 69 describe a second TRAMP complex, and show that the two TRAMP complexes have different substrate affinities.
  Article CAS PubMed PubMed Central Google Scholar
• Kadaba, S., Wang, X. & Anderson, J. T. Nuclear RNA surveillance in Saccharomyces cerevisiae: Trf4p-dependent polyadenylation of nascent hypomethylated tRNA and an aberrant form of 5S rRNA. RNA 12, 508?521 (2006). Extends the range of TRAMP substrates and shows that the complex acts on newly transcribed pre-tRNA.
  Article CAS PubMed PubMed Central 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 PubMed Google Scholar
• Gavin, A. C. et al. Proteome survey reveals modularity of the yeast cell machinery. Nature 440, 631?636 (2006).
  Article CAS PubMed Google Scholar
• Schilders, G., Raijmakers, R., Raats, J. M. & Pruijn, G. J. MPP6 is an exosome-associated RNA-binding protein involved in 5.8S rRNA maturation. Nucleic Acids Res. 33, 6795?6804 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Thomson, E. & Tollervey, D. Nop53p is required for late 60S ribosome subunit maturation and nuclear export in yeast. RNA 11, 1215?1224 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Granato, D. C. et al. Nop53p, an essential nucleolar protein that interacts with Nop17p and Nip7p, is required for pre-rRNA processing in Saccharomyces cerevisiae. FEBS J. 272, 4450?4463 (2005).
  Article CAS PubMed Google Scholar
• Brown, J. T., Bai, X. & Johnson, A. W. The yeast antiviral proteins Ski2p, Ski3p, and Ski8p exist as a complex in vivo. RNA 6, 449?457 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Inada, T. & Aiba, H. Translation of aberrant mRNAs lacking a termination codon or with a shortened 3′-UTR is repressed after initiation in yeast. EMBO J. 24, 1584?1595 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Cao, D. & Parker, R. Computational modeling and experimental analysis of nonsense-mediated decay in yeast. Cell 113, 533?45 (2003).
  Article CAS PubMed Google Scholar
• Wickner, R. B. Double-stranded and single-stranded RNA viruses of Saccharomyces cerevisiae. Annu. Rev. Microbiol. 46, 347?375 (1992).
  Article CAS PubMed Google Scholar
• Benard, L., Carroll, K., Valle, R. C., Masison, D. C. & Wickner, R. B. The ski7 antiviral protein is an EF1-α homolog that blocks expression of non-Poly(A) mRNA in Saccharomyces cerevisiae. J. Virol. 73, 2893?2900 (1999).
  Article CAS PubMed PubMed Central Google Scholar
• Ridley, S. P., Sommer, S. S. & Wickner, R. B. Superkiller mutations in Saccharomyces cerevisiae suppress exclusion of M2 double-stranded RNA by L-A-HN and confer cold sensitivity in the presence of M and L-A-HN. Mol. Cell. Biol. 4, 761?770 (1984).
  CAS PubMed PubMed Central Google Scholar
• Folichon, M. et al. Fate of mRNA extremities generated by intrinsic termination: detailed analysis of reactions catalyzed by ribonuclease II and poly(A) polymerase. Biochimie 87, 819?826 (2005).
  Article CAS PubMed Google Scholar
• Khemici, V. & Carpousis, A. J. The RNA degradosome and poly(A) polymerase of Escherichia coli are required in vivo for the degradation of small mRNA decay intermediates containing REP-stabilizers. Mol. Microbiol. 51, 777?790 (2004).
  Article CAS PubMed Google Scholar
• Kuai, L., Fang, F., Butler, J. S. & Sherman, F. Polyadenylation of rRNA in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 101, 8581?8586 (2004).
  Article CAS PubMed PubMed Central Google Scholar
• Haracska, L., Johnson, R. E., Prakash, L. & Prakash, S. Trf4 and Trf5 proteins of Saccharomyces cerevisiae exhibit poly(A) RNA polymerase activity but no DNA polymerase activity. Mol. Cell. Biol. 25, 10183?10189 (2005). Reports that both Trf4 and Trf5 are poly(A) polymerases.
  Article CAS PubMed PubMed Central Google Scholar
• West, S., Gromak, N., Norbury, C. J. & Proudfoot, N. J. Adenylation and exosome-mediated degradation of co-transcriptionally cleaved pre-messenger RNA in human cells Mol. Cell 21, 437?443 (2006). Evidence is presented that human mRNA molecules that fail to be correctly cleaved and polyadenylated are rapidly targeted by the exosome for degradation.
  Article CAS PubMed Google Scholar
• Teixeira, A. et al. Autocatalytic RNA cleavage in the human β-globin pre-mRNA promotes transcription termination. Nature 432, 526?530 (2004).
  Article CAS PubMed Google Scholar
• West, S., Gromak, N. & Proudfoot, N. J. Human 5′→3′ exonuclease Xrn2 promotes transcription termination at co-transcriptional cleavage sites. Nature 432, 522?525 (2004). Resolving a long-standing argument, West et al . show that cleavage occurs prior to transcriptional termination, the continuing RNA polymerase is then chased down by a 5′→3′ exonuclease that triggers its release.
  Article CAS PubMed Google Scholar
• Portnoy, V. et al. RNA polyadenylation in Archaea: not observed in Haloferax while the exosome polynucleotidylates RNA in Sulfolobus. EMBO Rep. 6, 1188?1193 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Yehudai-Resheff, S., Hirsh, M. & Schuster, G. Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts. Mol. Cell. Biol. 21, 5408?5416 (2001).
  Article CAS PubMed PubMed Central Google Scholar
• Mohanty, B. K. & Kushner, S. R. Polynucleotide phosphorylase functions both as a 3′→5′ exonuclease and a poly(A) polymerase in Escherichia coli. Proc. Natl Acad. Sci. USA 97, 11966?11971 (2000).
  Article CAS PubMed PubMed Central Google Scholar
• Bollenbach, T. J., Schuster, G. & Stern, D. B. Cooperation of endo- and exoribonucleases in chloroplast mRNA turnover. Prog. Nucleic Acid. Res. Mol. Biol. 78, 305?337 (2004).
  Article CAS PubMed Google Scholar
• Zhu, B. et al. The human PAF complex coordinates transcription with events downstream of RNA synthesis. Genes Dev. 19, 1668?1673 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Graham, A. C., Kiss, D. L. & Andrulis, E. D. Differential distribution of exosome subunits at the nuclear lamina and in cytoplasmic foci. Mol. Biol. Cell 17, 1399?1409 (2006). Reports that some exosome components show differential enrichments at distinct locations, which indicates that all human exosome components might not obligatorily function as a complex.
  Article CAS PubMed PubMed Central Google Scholar
• Rouhana, L. et al. Vertebrate GLD2 poly(A) polymerases in the germline and the brain. RNA 11, 1117?1130 (2005).
  Article CAS PubMed PubMed Central Google Scholar
• Kwak, J. E., Wang, L., Ballantyne, S., Kimble, J. & Wickens, M. Mammalian GLD-2 homologs are poly(A) polymerases. Proc. Natl Acad. Sci. USA 101, 4407?4412 (2004).
  Article CAS PubMed PubMed Central Google Scholar
• Dez, C., Houseley, J. & Tollervey, D. Surveillance of nuclear-restricted pre-ribosomes within a subnucleolar region of Saccharomyces cerevisiae. EMBO J. 25, 1534?1546 (2006). The authors show that defective pre-ribosomes are rapidly and completely degraded by the TRAMP and exosome in nucleolar 'No-bodies'.
  Article CAS PubMed PubMed Central Google Scholar
• Kadowaki, T. et al. Isolation and characterization of Saccharomyces cerevisiae mRNA transport-defective (mtr) mutants. J. Cell Biol. 126, 649?659 (1994).
  Article CAS PubMed Google Scholar