Article abstract
Nature Structural & Molecular Biology 15, 523 - 530 (2008)
Published online: 27 April 2008 | doi:10.1038/nsmb.1417
Mouse Eri1 interacts with the ribosome and catalyzes 5.8S rRNA processing
K Mark Ansel1,2,6, William A Pastor1,7, Nicola Rath3,7, Ariya D Lapan1,7, Elke Glasmacher3, Christine Wolf3, Laura C Smith1, Nikoletta Papadopoulou3,6, Edward D Lamperti1, Mamta Tahiliani1, Joachim W Ellwart3, Yujiang Shi4, Elisabeth Kremmer3, Anjana Rao1,5 & Vigo Heissmeyer3
Abstract
Eri1 is a 3'-to-5' exoribonuclease conserved from fission yeast to humans. Here we show that Eri1 associates with ribosomes and ribosomal RNA (rRNA). Ribosomes from Eri1–deficient mice contain 5.8S rRNA that is aberrantly extended at its 3' end, and Eri1, but not a catalytically inactive mutant, converts this abnormal 5.8S rRNA to the wild-type form in vitro and in cells. In human and murine cells, Eri1 localizes to the cytoplasm and nucleus, with enrichment in the nucleolus, the site of preribosome biogenesis. RNA binding residues in the Eri1 SAP and linker domains promote stable association with rRNA and thereby facilitate 5.8S rRNA 3' end processing. Taken together, our findings indicate that Eri1 catalyzes the final trimming step in 5.8S rRNA processing, functionally and spatially connecting this regulator of RNAi with the basal translation machinery.
- Immune Disease Institute, Harvard Medical School, 200 Longwood Avenue, Boston, Massachusetts 02115, USA.
- Department of Pediatrics, Childrens Hospital, 200 Longwood Avenue, Boston, Massachusetts 01125, USA.
- Helmholtz Center Munich, German Research Center for Environmental Health, Institute of Molecular Immunology, Marchioninistrasse 25, D-81377, Munich, Germany.
- Division of Endocrinology, Diabetes, and Hypertension, Department of Medicine and BCMP, Brigham and Women's Hospital and Harvard Medical School, 221 Longwood Avenue, Boston, Massachusetts 02115, USA.
- Department of Pathology, Harvard Medical School, 200 Longwood Avenue, Boston, Massachusetts 02115, USA.
- Present addresses: Sandler Asthma Basic Research Center, Department of Microbiology and Immunology, University of California San Francisco, 513 Parnassus Avenue, Box 0414, San Francisco, California 94143, USA (K.M.A.) and Institute for Genetics, University of Cologne, Zulpicher Strasse 47, D-50674 Cologne, Germany (N.P.).
- These authors contributed equally to this work.
Correspondence to: Vigo Heissmeyer3 e-mail: vigo.heissmeyer@helmholtz-muenchen.de
Correspondence to: K Mark Ansel1,2,6 e-mail: mark.ansel@ucsf.edu
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