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Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.
Structural and biochemical characterization of the yeast exosome component Rrp40.
EMBO Rep. 8, 63-69 (2007)
The exosome is a protein complex that is important in both degradation and 3'-processing of eukaryotic RNAs. We present the crystal structure of the Rrp40 exosome subunit from Saccharomyces cerevisiae at a resolution of 2.2 A. The structure comprises an S1 domain and an unusual KH (K homology) domain. Close packing of the S1 and KH domains is stabilized by a GxNG sequence, which is uniquely conserved in exosome KH domains. Nuclear magnetic resonance data reveal the presence of a manganese-binding site at the interface of the two domains. Isothermal titration calorimetry shows that Rrp40 and archaeal Rrp4 alone have very low intrinsic affinity for RNA. The affinity of an archaeal core exosome for RNA is significantly increased in the presence of the S1-KH subunit Rrp4, indicating that multiple subunits might contribute to cooperative binding of RNA substrates by the exosome.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
exosome; RNA degradation; exonuclease; S1 domain; KH domain
ISSN (print) / ISBN
1469-221X
e-ISSN
1469-3178
Journal
EMBO Reports
Quellenangaben
Volume: 8,
Issue: 1,
Pages: 63-69
Publisher
EMBO Press
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)