Abstract
The exosome complex of 3′→5′ exoribonucleases functions in both the precise processing of 3′ extended precursor molecules to mature stable RNAs and the complete degradation of other RNAs. Both processing and degradative activities of the exosome depend on additional cofactors, notably the putative RNA helicases Mtr4p and Ski2p. It is not known how these factors regulate exosome function or how the exosome distinguishes RNAs destined for processing events from substrates that are to be completely degraded. Here we review the available data concerning the modes of action of the exosome and relate these to possible structural arrangements for the complex. As no detailed structural data are yet available for the exosome complex, or any of its constituent enzymes, this discussion will rely heavily on rather speculative models.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 12 print issues and online access
$189.00 per year
only $15.75 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Mian, S. Nucleic Acids Res. 25, 3187–3195 (1997).
Moser, M.J., Holley, W.R., Chatterjee, A. & Mian, S. Nucleic Acids Res. 25, 5110–5118 (1997).
Mitchell, P., Petfalski, E., Schevchenko, A., Mann, M. & Tollervey, D. Cell 91, 457–466 (1997).
Allmang, C. et al. Genes Dev. 13, 2148–2158 (1999).
Deutscher, M.P. J. Bacteriol. 175, 4577–4583 (1993).
Burkard, K.T.D. & Butler, J.S. Mol. Cell. Biol. 20, 604–616 (2000).
Allmang, C., et al. EMBO J. 18, 5399–5410 (1999).
Allmang, C., Mitchell, P., Petfalski, E. & Tollervey, D. Nucleic Acids Res. 28, 1684–1691 (2000).
Kufel, J. et al. Mol. Cell. Biol. 20, 5415–5424 (2000).
Bousquet-Antonelli, C., Presutti, C. & Tollervey, D. Cell, in the press (2000).
van Hoof, A., Lennertz, P. & Parker, R. Mol. Cell. Biol. 20, 441–452 (2000).
de la Cruz, J., Kressler, D., Tollervey, D. & Linder, P. EMBO J. 17, 1128–1140 (1998).
Jacobs Anderson, J.S. & Parker, R. EMBO J. 17, 1497–1506 (1998).
van Hoof, A. & Parker, R. Cell 99, 347–350 (1999).
Baker, R., Harris, K. & Zhang, K. Genetics 149, 73–85 (1998).
Shiomi, T. et al. J. Biochem. 123, 883–890 (1998).
Baumeister, W., Walz, J., Zühl, F. & Seemüller, E. Cell 92, 367–380 (1998).
DeMartino, G.N. & Slaughter, C.A. J. Biol. Chem. 274, 22123–22126 (1999).
Rubin, D.M., Glickman, M.H., Larsen, C.N., Dhruvakumar, S. & Finley, D. EMBO J. 17, 4909–4919 (1998).
Palombella, V.J., Rando, O.J., Goldberg, A.L. & Maniatis, T. Cell 78, 773–785 (1994).
Sears, C., Olesen, J., Rubin, D., Finley, D. & Maniatis, T. J. Biol. Chem. 273, 1409–1419 (1998).
Lin, L., DeMartino, G.N. & Greene, W.C. Cell 92, 819–828 (1998).
Lin, L. & Ghosh, S. Mol. Cell. Biol. 16, 2248–2254 (1996).
Mitchell, P., Petfalski, E. & Tollervey, D. Genes Dev. 10, 502–513 (1996).
Ost Kelly, K. & Deutscher, M.P. J. Biol. Chem. 267, 17153–17158 (1992).
Grunberg-Manago, M., Ortiz, P.J. & Ochoa, S. Science 122, 907–910 (1955).
Py, B., Higgins, C.F., Krisch, H.M. & Carpousis, A.J. Nature 381, 169–172 (1996).
Miczak, A., Kaberdin, V. R., Wei, C.-L. & Lin-Chao, S. Proc. Natl. Acad. Sci. USA 93, 3865–3869 (1996).
Cheng, Z.-F., Zuo, Y., Li, Z., Rudd, K.E. & Deutscher, M.P. J. Biol. Chem. 272, 14077–14080 (1998).
Stevens, A. J. Biol. Chem. 255, 3080–3085 (1979).
Kenna, M., Stevens, A., McCammon, M. & Douglas, M.G. Mol. Cell. Biol. 13, 341–350 (1993).
Hilleren, P. & Parker, R. RNA 5, 711–719 (1999).
González, C.I., Ruiz-Echevarria, M.J., Vasudevan, S., Henry, M.F. & Peltz, S.W. Mol. Cell 5, 489–499 (2000).
Le Hir, H., Moore, M.J. & Maquat, L.E. Genes Dev. 14, 1098–1108 (2000).
Acknowledgements
We would like to thank A. van Hoof and R. Parker for sharing data prior to publication. This work is funded by the Wellcome Trust.
Author information
Authors and Affiliations
Corresponding authors
Rights and permissions
About this article
Cite this article
Mitchell, P., Tollervey, D. Musing on the structural organization of the exosome complex. Nat Struct Mol Biol 7, 843–846 (2000). https://doi.org/10.1038/82817
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/82817
This article is cited by
-
Global analysis of uncapped mRNA changes under drought stress and microRNA-dependent endonucleolytic cleavages in foxtail millet
BMC Plant Biology (2015)
-
Quality control of spliced mRNAs requires the shuttling SR proteins Gbp2 and Hrb1
Nature Communications (2014)
-
The Zea mays glycine-rich RNA-binding protein MA16 is bound to a ribonucleotide(s) by a stable linkage
Journal of Plant Research (2012)
-
Human polynucleotide phosphorylase (hPNPaseold-35): an evolutionary conserved gene with an expanding repertoire of RNA degradation functions
Oncogene (2011)
-
Dissecting mechanisms of nuclear mRNA surveillance in THO/sub2 complex mutants
The EMBO Journal (2007)