Abstract:
:The exosome is a complex of eleven subunits in yeast, involved in RNA processing and degradation. Despite the extensive in vivo functional studies of the exosome, little information is yet available on the structure of the complex and on the RNase and RNA binding activities of the individual subunits. The current model for the exosome structure predicts the formation of a heterohexameric RNase PH ring, bound on one side by RNA binding subunits, and on the opposite side by hydrolytic RNase subunits. Here, we report protein-protein interactions within the exosome, confirming the predictions of constituents of the RNase PH ring, and show some possible interaction interfaces between the other subunits. We also show evidence that Rrp40p can bind RNA in vitro, as predicted by sequence analysis.
journal_name
Biochimiejournal_title
Biochimieauthors
Luz JS,Tavares JR,Gonzales FA,Santos MC,Oliveira CCdoi
10.1016/j.biochi.2007.01.011subject
Has Abstractpub_date
2007-05-01 00:00:00pages
686-91issue
5eissn
0300-9084issn
1638-6183pii
S0300-9084(07)00022-3journal_volume
89pub_type
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