The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila

Nature

Volumn 420, Issue 6917, 2002, Pages 837-841

  Andrulis, Erik D ^a   Werner, Janis ^a   Nazarian, Arpi ^b   Erdjument Bromage, Hediye ^b   Tempst, Paul ^b   Lis, John T ^a  

^a Department of Obstetrics Gynecology   (United States)

^b MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASSAYS; DEGRADATION; GENES;

POLYMERASE;

RNA;

EXORIBONUCLEASE; MESSENGER RNA PRECURSOR; RNA; RNA POLYMERASE II;

RNA;

ARTICLE; CATALYSIS; CHROMATOGRAPHY; DROSOPHILA; ENZYME ANALYSIS; GENE INDUCTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; RNA DEGRADATION; RNA PROCESSING;

ANIMALS; CELL LINE; CHROMOSOMAL PROTEINS, NON-HISTONE; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; EXORIBONUCLEASES; GENE EXPRESSION REGULATION; GENES, INSECT; HEAT-SHOCK PROTEINS; MACROMOLECULAR SUBSTANCES; NUCLEAR PROTEINS; PEPTIDE ELONGATION FACTORS; PRECIPITIN TESTS; PROTEIN BINDING; PROTEIN SUBUNITS; RNA POLYMERASE II; RNA PRECURSORS; RNA PROCESSING, POST-TRANSCRIPTIONAL; TRANSCRIPTION, GENETIC; TRANSCRIPTIONAL ELONGATION FACTORS;

EID: 0037180825     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01181     Document Type: Article

References (23)

1. Hirose, Y. & Manley, J. L. RNA polymerase II and the integration of nuclear events. Genes Dev. 14, 1415-1429 (2000).
2. Bentley, D. Coupling RNA polymerase II transcription with pre-mRNA processing. Curr Opin. Cell Biol. 11, 347-351 (1999).
3. Proudfoot, N. J., Furger, A. & Dye, M. J. Integrating mRNA processing with transcription. Cell 108, 501-512 (2002).
4. Kaplan, C. D., Morris, J. R., Wu, C. & Winston, F. Spt5 and spt6 are associated with active transcription and have characteristics of general elongation factors in D. melanogaster. Genes Dev. 14, 2623-2634 (2000).
5. Andrulis, E. D., Guzman, E., Doring, P., Werner, I. & Lis, J. T. High-resolution localization of Drosophila Spt5 and Spt6 at heat shock genes in vivo: Roles in promoter proximal pausing and transcription elongation. Genes Dev. 14, 2635-2649 (2000).
6. 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).
7. Butler, J. S. The yin and yang of the exosome. Trends Cell Biol. 12, 90-96 (2002).
8. Bousquet-Antonelli, C., Presutti, C. & Tollervey, D. Identification of a regulated pathway for nuclear pre-mRNA turnover. Cell 102, 765-775 (2000).
9. 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).
10. Torchet, C. et al. Processing of 3′-extended read-through transcripts by the exosome can generate functional mRNAs. Mol. Cell 9, 1285-1296 (2002).
11. Hartzog, G. A., Wada, T., Honda, H. & Winston, F. Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae. Genes Dev. 12, 357-369 (1998).
12. Bortvin, A. & Winston, F. Evidence that Spt6p controls chromatin structure by a direct interaction with histories. Science 272, 1473-1476 (1996).
13. Gavin, A. C. et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415, 141-147 (2002).
14. Allmang, C. et al. The yeast exosome and human PM-Scl are related complexes of 3′ - 5′ exonucleases. Genes Dev. 13, 2148-2158 (1999).
15. Mitchell, P., Petfalski, E., Shevchenko, A., Mann, M. & Tollervey, D. The exosome: A conserved eukaryotic RNA processing complex containing multiple 3′ - 5′ exoribonucleases. Cell 91, 457-466 (1997).
16. Mitchell, P. & Tollervey, D. Musing on the structural organization of the exosome complex. Nature Struct. Biol. 7, 843-846 (2000).
17. Lis, J. T., Mason, P., Peng, J. & Price, D. H. P-TFFb kinase recruitment and function at heat shock loci. Genes Dev. 14, 792-803 (2000).
18. Erdjument-Bromage, H. et al. Examination of micro-tip reversed-phase liquid chromatographic extraction of peptide pools for mass spectrometric analysis. J. Chromatogr. A 826, 167-181 (1998).
19. Geromanos, S., Freckleton, G. & Tempst, P. Tuning of an electrospray ionization source for maximum peptide-ion transmission into a mass spectrometer. Anal. Chem. 72, 777-790 (2000).
20. Mann, M., Hojrup, P. & Roepstorff, P. Use of mass spectrometric molecular weight information to identify proteins in sequence databases. Biol. Mass. Spectrom. 22, 338-345 (1993).
21. Fenyo, D., Qin, J. & Chait, B. T. Protein identification using mass spectrometric information. Electrophoresis 19, 998-1005 (1998).
22. Park, J. M., Worner, J., Kim, J. M., Lis, J. T. & Kim, Y. J. Mediator, not holoenzyme, is directly recruited to the heat shock promoter by HSF upon heat shock. Mol. Cell 8, 9-19 (2001).
23. Shopland, L. S. & Lis, J. T. HSF recruitment and loss at most Drosophila heat shock loci is coordinated and depends on proximal promoter sequences. Chromosoma 105, 158-171 (1996).