Ribosome-stalk biogenesis is coupled with recruitment of nuclear-export factor to the nascent 60S subunit

Nature Structural & Molecular Biology
Anshuk SarkarEd Hurt

Abstract

Nuclear export of preribosomal subunits is a key step during eukaryotic ribosome formation. To efficiently pass through the FG-repeat meshwork of the nuclear pore complex, the large pre-60S subunit requires several export factors. Here we describe the mechanism of recruitment of the Saccharomyces cerevisiae RNA-export receptor Mex67-Mtr2 to the pre-60S subunit at the proper time. Mex67-Mtr2 binds at the premature ribosomal-stalk region, which later during translation serves as a binding platform for translational GTPases on the mature ribosome. The assembly factor Mrt4, a structural homolog of cytoplasmic-stalk protein P0, masks this site, thus preventing untimely recruitment of Mex67-Mtr2 to nuclear pre-60S particles. Subsequently, Yvh1 triggers Mrt4 release in the nucleus, thereby creating a narrow time window for Mex67-Mtr2 association at this site and facilitating nuclear export of the large subunit. Thus, a spatiotemporal mark on the ribosomal stalk controls the recruitment of an RNA-export receptor to the nascent 60S subunit.

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Citations

Jan 24, 2017·Nature Structural & Molecular Biology·Chengying MaNing Gao
Nov 28, 2017·Nature Communications·Lisa FrommEd Hurt
Oct 31, 2017·Nature Structural & Molecular Biology·Anshuk SarkarEd Hurt
Nov 24, 2018·Nature Reviews. Molecular Cell Biology·Sebastian Klinge, John L Woolford
Sep 8, 2017·Nature Structural & Molecular Biology·Cohue PeñaVikram Govind Panse
Jun 14, 2018·The Journal of Clinical Endocrinology and Metabolism·Christine M Burt SolorzanoChristopher R McCartney
Mar 1, 2019·Nature Communications·Yi ZhouDavid W Taylor
Jan 9, 2020·The Biochemical Journal·Asaf Ashkenazy-TitelmanRalph H Kehlenbach
Dec 4, 2020·International Journal of Molecular Sciences·Helge PaternogaEd Hurt
Jun 6, 2017·Trends in Biochemical Sciences·Dieter KresslerJochen Baßler

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