Proofreading of pre-40S ribosome maturation by a translation initiation factor and 60S subunits

被引：146

作者：

Lebaron, Simon ^{[1
]}

Schneider, Claudia ^{[1
,2
]}

van Nues, Robert W. ^{[2
]}

Swiatkowska, Agata ^{[1
]}

Walsh, Dietrich ^{[1
]}

Boettcher, Bettina ^{[1
,3
]}

Granneman, Sander ^{[4
]}

Watkins, Nicholas J. ^{[2
]}

Tollervey, David ^{[1
]}

机构：

[1] Univ Edinburgh, Wellcome Trust Ctr Cell Biol, Edinburgh, Midlothian, Scotland

[2] Newcastle Univ, Inst Cell & Mol Biosci, Newcastle Upon Tyne NE1 7RU, Tyne & Wear, England

[3] Univ Edinburgh, Inst Struct & Mol Biol, Edinburgh, Midlothian, Scotland

[4] Univ Edinburgh, Edinburgh, Midlothian, Scotland

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2012年 / 19卷 / 08期

基金：

英国惠康基金;

关键词：

INTERNAL TRANSCRIBED SPACER-1; SACCHAROMYCES-CEREVISIAE; CYTOPLASMIC MATURATION; ESCHERICHIA-COLI; FACTOR EIF5B; PIN DOMAIN; RNA; YEAST; BIOGENESIS; PROTEIN;

D O I：

10.1038/nsmb.2308

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：

In the final steps of yeast ribosome synthesis, immature translation-incompetent pre-40S particles that contain 20S pre-rRNA are converted to the mature translation-competent subunits containing the 18S rRNA. An assay for 20S pre-rRNA cleavage in purified pre-40S particles showed that cleavage by the PIN domain endonuclease Nob1 was strongly stimulated by the GTPase activity of Fun12, the yeast homolog of cytoplasmic translation initiation factor elF5b. Cleavage of the 20S pre-rRNA was also inhibited in vivo and in vitro by blocking binding of Fun12 to the 25S rRNA through specific methylation of its binding site. Cleavage competent pre-40S particles stably associated with Fun12 and formed 80S complexes with 60S ribosomal subunits. We propose that recruitment of 60S subunits promotes GTP hydrolysis by Fun12, leading to structural rearrangements within the pre-40S particle that bring Nob1 and pre-rRNA cleavage site together.

引用

页码：744 / 753

页数：10

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