The ribosome assembly factor Nop53 has a structural role in the formation of nuclear pre-60S intermediates,affecting late maturation events

项目来源

巴西圣保罗研究基金(FAPESP)

项目主持人

Carla Columbano de Oliveira

项目受资助机构

Instituto de Química.Universidade de São Paulo.São Paulo,SP,Brazil

立项年度

2021

立项时间

未公开

项目编号

21/05163-1

研究期限

未知 / 未知

项目级别

国家级

受资助金额

未知

学科

Biological Sciences

学科代码

未公开

基金类别

Regular Research Grants-Publications-Scientific article

关键词

Controle de expressão gênica ; Processamento de RNA ; Exossomos ; Controle da expressão gênica ;

参与者

未公开

参与机构

未公开

项目标书摘要:Eukaryotic ribosome biogenesis is an elaborate process during which ribosomal proteins assemble with the pre-rRNA while it is being processed and folded.Hundreds of assembly factors(AF)are required and transiently recruited to assist the sequential remodeling events.One of the most intricate ones is the stepwise removal of the internal transcribed spacer 2(ITS2),between the 5.8S and 25S rRNAs,that constitutes together with five AFs the pre-60S"foot".In the transition from nucleolus to nucleoplasm,Nop53 replaces Erb1 at the basis of the foot and recruits the RNA exosome for the ITS2 cleavage and foot disassembly.Here we comprehensively analyze the impact of Nop53 recruitment on the pre-60S compositional changes.We show that depletion of Nop53,different from nop53 mutants lacking the exosome-interacting motif,not only causes retention of the unprocessed foot in late pre-60S intermediates but also affects the transition from nucleolar state E particle to subsequent nuclear stages.Additionally,we reveal that Nop53 depletion causes the impairment of late maturation events such as Yvh1 recruitment.In light of recently described pre-60S cryo-EM structures,our results provide biochemical evidence for the structural role of Nop53 rearranging and stabilizing the foot interface to assist the Nog2 particle formation.(AU)

Application Abstract: Eukaryotic ribosome biogenesis is an elaborate process during which ribosomal proteins assemble with the pre-rRNA while it is being processed and folded.Hundreds of assembly factors(AF)are required and transiently recruited to assist the sequential remodeling events.One of the most intricate ones is the stepwise removal of the internal transcribed spacer 2(ITS2),between the 5.8S and 25S rRNAs,that constitutes together with five AFs the pre-60S"foot".In the transition from nucleolus to nucleoplasm,Nop53 replaces Erb1 at the basis of the foot and recruits the RNA exosome for the ITS2 cleavage and foot disassembly.Here we comprehensively analyze the impact of Nop53 recruitment on the pre-60S compositional changes.We show that depletion of Nop53,different from nop53 mutants lacking the exosome-interacting motif,not only causes retention of the unprocessed foot in late pre-60S intermediates but also affects the transition from nucleolar state E particle to subsequent nuclear stages.Additionally,we reveal that Nop53 depletion causes the impairment of late maturation events such as Yvh1 recruitment.In light of recently described pre-60S cryo-EM structures,our results provide biochemical evidence for the structural role of Nop53 rearranging and stabilizing the foot interface to assist the Nog2 particle formation.(AU)

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