000030555 001__ 30555
000030555 005__ 20131002114017.0
000030555 0248_ $$aoai:doc.rero.ch:20121108085713-EH$$punifr$$ppostprint$$prero_explore$$zcdu34$$zthesis_urn$$zcdu57$$zreport$$zthesis$$zbook$$zjournal$$zcdu16$$zpreprint$$zcdu1$$zdissertation
000030555 041__ $$aeng
000030555 080__ $$a57
000030555 100__ $$aKressler, Dieter$$uBiochemie Zentrum der Universität Heidelberg, Germany - Unit of Biochemistry, Department of Biology, University of Fribourg, Switzerland
000030555 245__ $$9eng$$aSynchronizing nuclear import of ribosomal proteins with ribosome assembly
000030555 520__ $$9eng$$aRibosomal proteins are synthesized in the cytoplasm, before nuclear import and assembly with ribosomal RNA (rRNA). Little is known about coordination of nucleocytoplasmic transport with ribosome assembly. Here, we identify a transport adaptor, symportin 1 (Syo1), that facilitates synchronized coimport of the two 5S-rRNA binding proteins Rpl5 and Rpl11. In vitro studies revealed that Syo1 concomitantly binds Rpl5-Rpl11 and furthermore recruits the import receptor Kap104. The Syo1-Rpl5-Rpl11 import complex is released from Kap104 by RanGTP and can be directly transferred onto the 5S rRNA. Syo1 can shuttle back to the cytoplasm by interaction with phenylalanine-glycine nucleoporins. X-ray crystallography uncovered how the α-solenoid symportin accommodates the Rpl5 amino terminus, normally bound to 5S rRNA, in an extended groove. Symportin-mediated coimport of Rpl5-Rpl11 could ensure coordinated and stoichiometric incorporation of these proteins into pre-60S ribosomes.
000030555 700__ $$aBange, Gert$$uBiochemie Zentrum der Universität Heidelberg, Germany
000030555 700__ $$aOgawa, Yutaka$$uBiomolecular Networks Laboratories, Graduate School of Frontier Biosciences, Osaka University, Japan.
000030555 700__ $$aStjepanovic, Goran$$uBiochemie Zentrum der Universität Heidelberg, Germany
000030555 700__ $$aBradatsch, Bettina$$uBiochemie Zentrum der Universität Heidelberg, Germany
000030555 700__ $$aPratte, Dagmar$$uUnit of Biochemistry, Department of Biology, University of Fribourg, Switzerland
000030555 700__ $$aAmlacher, Stefan$$uBiochemie Zentrum der Universität Heidelberg, Germany
000030555 700__ $$aStrauß, Daniela$$uBiochemie Zentrum der Universität Heidelberg, Germany
000030555 700__ $$aYoneda, Yoshihiro$$uBiomolecular Networks Laboratories, Graduate School of Frontier Biosciences, Osaka University, Japan.
000030555 700__ $$aKatahira, Jun$$uBiomolecular Networks Laboratories, Graduate School of Frontier Biosciences, Osaka University, Japan.
000030555 700__ $$aSinning, Irmgard$$uBiochemie Zentrum der Universität Heidelberg, Germany
000030555 700__ $$aHurt, Ed$$uBiochemie Zentrum der Universität Heidelberg, Germany
000030555 773__ $$g2012/338/6107/666-671$$tScience
000030555 775__ $$gPublished version$$ohttp://dx.doi.org/10.1126/science.1226960
000030555 8564_ $$fkre_sni.pdf$$qapplication/pdf$$s554283$$uhttp://doc.rero.ch/record/30555/files/kre_sni.pdf$$yorder:1$$zpdf
000030555 8564_ $$fkre_sni_sm.pdf$$qapplication/pdf$$s3639333$$uhttp://doc.rero.ch/record/30555/files/kre_sni_sm.pdf$$yorder:2$$zSupplementary material
000030555 918__ $$aFaculté des sciences$$bDécanat, Ch. du Musée 6A, 1700 Fribourg$$cBiologie
000030555 919__ $$aUniversité de Fribourg$$bFribourg$$ddoc.support@rero.ch
000030555 980__ $$aPOSTPRINT$$bUNIFR$$fART_JOURNAL
000030555 990__ $$a20121108085713-EH