OpenSSL SSL_connect: Connection reset by peer in connection to v2.sherpa.ac.uk:443 PuSH - Publication Server of Helmholtz Zentrum München: Structural and biochemical characterization of the yeast exosome component Rrp40.

PuSH - Publication Server of Helmholtz Zentrum München

Oddone, A.* ; Lorentzen, E.* ; Basquin, J.* ; Gasch, A.* ; Rybin, V.* ; Conti, E.* ; Sattler, M.

Structural and biochemical characterization of the yeast exosome component Rrp40.

EMBO Rep. 8, 63-69 (2007)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
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
Corresponding Author
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 Article Number: , Supplement: ,
Publisher EMBO Press
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)