Exosome substrate targeting: the long and short of it. (11th August 2014)

• Record Type: Journal Article
• Authors: Mitchell, Phil
• Is Part Of: Biochemical Society transactions. Volume 42:Number 4(2014)
• Page Start: 1129
• Page End: 1134
• Publication Date: 2014-08-11
• Subjects: Dis3 -- exosome -- ribonuclease -- rRNA-processing protein 44 (Rrp44) -- rRNA-processing protein 6 (Rrp6) -- Ski -- Trf4–Air2–Mtr4 polyadenylation complex (TRAMP complex); Biochemistry -- Congresses; 572
• DOI: 10.1042/BST20140088
• Languages: English
• ISSNs: 0300-5127

Abstract

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.