The Efg1-Bud22 dimer associates with the U14 snoRNP contacting the 5′ rRNA domain of an early 90S pre-ribosomal particle

被引：0

作者：

Beine-Golovchuk, Olga ^{[1
]}

Kallas, Martina ^{[1
]}

Kunze, Ruth ^{[1
]}

Griesel, Sabine ^{[1
]}

Bassler, Jochen ^{[1
]}

机构：

[1] Univ Heidelberg BZH, Biochem Zentrum, Neuenheimer Feld 328, D-69120 Heidelberg, Germany

来源：

NUCLEIC ACIDS RESEARCH | 2024年 / 52卷 / 01期

基金：

欧洲研究理事会;

关键词：

SMALL NUCLEOLAR RNA; HELICASE DBP4; U3; SNORNA; PROTEINS; IDENTIFICATION; PRERIBOSOME; BIOGENESIS; PROCESSOME; VERSATILE; STEPWISE;

D O I：

10.1093/nar/gkad1109

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：

The DEAD-box helicase Dbp4 plays an essential role during the early assembly of the 40S ribosome, which is only poorly understood to date. By applying the yeast two-hybrid method and biochemical approaches, we discovered that Dbp4 interacts with the Efg1-Bud22 dimer. Both factors associate with early pre-90S particles and smaller complexes, each characterized by a high presence of the U14 snoRNA. A crosslink analysis of Bud22 revealed its contact to the U14 snoRNA and the 5 ' domain of the nascent 18S rRNA, close to its U14 snoRNA hybridization site. Moreover, depletion of Bud22 or Efg1 specifically affects U14 snoRNA association with pre-ribosomal complexes. Accordingly, we concluded that the role of the Efg1-Bud22 dimer is linked to the U14 snoRNA function on early 90S ribosome intermediates chaperoning the 5 ' domain of the nascent 18S rRNA. The successful rRNA folding of the 5 ' domain and the release of Efg1, Bud22, Dpb4, U14 snoRNA and associated snoRNP factors allows the subsequent recruitment of the Kre33-Bfr2-Enp2-Lcp5 module towards the 90S pre-ribosome. Graphical Abstract

引用

页码：431 / 447

页数：17