Mitchell, P. (2014) Exosome substrate targeting: the long and short of it. Biochemical Society Transactions, 42. 1129 - 1134. ISSN 0300-5127
Abstract
The exosome ribonuclease complex functions in both the limited trimming of the 3′-ends of nuclear substrates during RNA processing events and the complete destruction of nuclear and cytoplasmic RNAs. The two RNases of the eukaryotic exosome, Rrp44 (rRNA-processing protein 44) and Rrp6, are bound at either end of a catalytically inert cylindrical core. RNA substrates are threaded through the internal channel of the core to Rrp44 by RNA helicase components of the nuclear TRAMP complex (Trf4–Air2–Mtr4 polyadenylation complex) or the cytoplasmic Ski (superkiller) complex. Recent studies reveal that Rrp44 can also associate directly with substrates via channel-independent routes. Although the substrates of the exosome are known, it is not clear whether specific substrates are restricted to one or other pathway. Data currently available support the model that processed substrates are targeted directly to the catalytic subunits, whereas at least some substrates that are directed towards discard pathways must be threaded through the exosome core.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2014 Biochemical Society. This is an author produced version of a paper subsequently published in Biochemical Society Transactions. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | Dis3; exosome; ribonuclease; rRNA-processing protein 44 (Rrp44); rRNA-processing protein 6 (Rrp6); Ski; Trf4-Air2-Mtr4 polyadenylation complex (TRAMP complex) |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 08 Oct 2015 15:37 |
Last Modified: | 21 Mar 2018 18:21 |
Published Version: | http://dx.doi.org/10.1042/BST20140088 |
Status: | Published |
Publisher: | Portland Press |
Refereed: | Yes |
Identification Number: | 10.1042/BST20140088 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:89311 |