Mouse Eri1 interacts with the ribosome and catalyzes 5.8S rRNA processing

被引：55

作者：

Ansel, K. Mark ^{[1
,4
]}

Pastor, William A. ^{[4
]}

Rath, Nicola ^{[2
]}

Lapan, Ariya D. ^{[4
]}

Glasmacher, Elke ^{[2
]}

Wolf, Christine ^{[2
]}

Smith, Laura C. ^{[4
]}

Papadopoulou, Nikoletta ^{[2
]}

Lamperti, Edward D. ^{[4
]}

Tahiliani, Mamta ^{[4
]}

Ellwart, Joachim W. ^{[2
]}

Shi, Yujiang

Kremmer, Elisabeth ^{[2
]}

Rao, Anjana ^{[3
,4
]}

Heissmeyer, Vigo ^{[2
]}

机构：

[1] Childrens Hosp, Dept Pediat, Boston, MA 01125 USA

[2] German Res Ctr Environm Hlth, Helmholtz Ctr Munich, Inst Mol Immunol, D-81377 Munich, Germany

[3] Harvard Med Sch, Dept Pathol, Boston, MA 02115 USA

[4] Harvard Med Sch, Immune Dis Inst, Boston, MA 02115 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2008年 / 15卷 / 05期

关键词：

D O I：

10.1038/nsmb.1417

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：523 / 530

页数：8

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