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Title | Ribosome-stalk biogenesis is coupled with recruitment of nuclear-export factor to the nascent 60S subunit. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 23, Issue 12, Page 1074-1082, Year 2016 |
Publish date | Oct 24, 2016 |
Authors | Anshuk Sarkar / Markus Pech / Matthias Thoms / Roland Beckmann / Ed Hurt / |
PubMed 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 ...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. |
External links | Nat Struct Mol Biol / PubMed:27775710 |
Methods | EM (single particle) |
Resolution | 7.4 Å |
Structure data | EMDB-4096: |
Source |
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