Abstract：
:The exosome plays key roles in RNA maturation and surveillance, but it is unclear how target RNAs are identified. We report the functional characterization of the yeast exosome component Rrp44, a member of the RNase II family. Recombinant Rrp44 and the purified TRAMP polyadenylation complex each specifically recognized tRNA(i)(Met) lacking a single m(1)A(58) modification, even in the presence of a large excess of total tRNA. This tRNA is otherwise mature and functional in translation in vivo but is presumably subtly misfolded. Complete degradation of the hypomodified tRNA required both Rrp44 and the poly(A) polymerase activity of TRAMP. The intact exosome lacking only the catalytic activity of Rrp44 failed to degrade tRNA(i)(Met), showing this to be a specific Rrp44 substrate. Recognition of hypomodified tRNA(i)(Met) by Rrp44 is genetically separable from its catalytic activity on other substrates, with the mutations mapping to distinct regions of the protein.
journal_name
Mol Celljournal_title
Molecular cellauthors
Schneider C,Anderson JT,Tollervey Ddoi
10.1016/j.molcel.2007.06.006subject
Has Abstractpub_date
2007-07-20 00:00:00pages
324-31issue
2eissn
1097-2765issn
1097-4164pii
S1097-2765(07)00370-Xjournal_volume
27pub_type
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