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-Structure paper
| Title | Architecture of the yeast Rrp44 exosome complex suggests routes of RNA recruitment for 3' end processing. |
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| Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 104, Issue 43, Page 16844-16849, Year 2007 |
| Publish date | Oct 23, 2007 |
 Authors | Hong-Wei Wang / Jianjun Wang / Fang Ding / Kevin Callahan / Matthew A Bratkowski / J Scott Butler / Eva Nogales / Ailong Ke /  |
| PubMed Abstract | The eukaryotic core exosome (CE) is a conserved nine-subunit protein complex important for 3' end trimming and degradation of RNA. In yeast, the Rrp44 protein constitutively associates with the CE ...The eukaryotic core exosome (CE) is a conserved nine-subunit protein complex important for 3' end trimming and degradation of RNA. In yeast, the Rrp44 protein constitutively associates with the CE and provides the sole source of processive 3'-to-5' exoribonuclease activity. Here we present EM reconstructions of the core and Rrp44-bound exosome complexes. The two-lobed Rrp44 protein binds to the RNase PH domain side of the exosome and buttresses the bottom of the exosome-processing chamber. The Rrp44 C-terminal body part containing an RNase II-type active site is anchored to the exosome through a conserved set of interactions mainly to the Rrp45 and Rrp43 subunit, whereas the Rrp44 N-terminal head part is anchored to the Rrp41 subunit and may function as a roadblock to restrict access of RNA to the active site in the body region. The Rrp44-exosome (RE) architecture suggests an active site sequestration mechanism for strict control of 3' exoribonuclease activity in the RE complex. |
 External links | Proc Natl Acad Sci U S A / PubMed:17942686 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 19.0 - 23.0 Å |
| Structure data |  EMDB-1438:  EMDB-1439: |
| Source |
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Saccharomyces cerevisiae (brewer's yeast)