A pre-ribosome-associated HEAT-repeat protein is required for export of both ribosomal subunits

被引:101
作者
Oeffinger, M
Dlakic, M
Tollervey, D [1 ]
机构
[1] Univ Edinburgh, Wellcome Trust Ctr Cell Biol, Edinburgh EH9 3JR, Midlothian, Scotland
[2] Montana State Univ, Dept Microbiol, Bozeman, MT 59717 USA
基金
英国惠康基金;
关键词
ribosome export;
D O I
10.1101/gad.285604
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Rrp12p (Ypl012w) is unusual among characterized ribosome synthesis factors in being associated with late precursors to both the 40S and 60S subunits. Rrp12p is predominately nuclear with nucleolar enrichment at steady state, but shuttled between the nucleus and cytoplasm in a heterokaryon assay. Strains depleted of Rrp12p are impaired in the nuclear export of both ribosomal subunits. Sequence analysis combined with fold recognition and modeling showed that Rrp12p is a member of a family of pre-ribosome-associated HEAT-repeat proteins. Like other HEAT-repeat transport factors, Rrp12p binds in vitro to nucleoporin FG-repeats of both the GLFG and FXFG families and to the GTPase Gsp1p (yeast RAN). Rrp12p also showed robust in vitro binding to a pre-rRNA transcript, in addition to poly(A) and poly(U). We propose that Rrp12p binds to the RNA components of the pre-ribosomes and promotes export of both subunits via its interactions with the nucleoporins and Gsp1p.
引用
收藏
页码:196 / 209
页数:14
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