The ribosome assembly factor Nop53 has a structura... - BV FAPESP
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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Bagatelli, Felipe F. M. [1] ; de Luna Vitorino, Francisca N. [2, 3] ; da Cunha, Julia P. C. [2, 3] ; Oliveira, Carla C. [1]
Total Authors: 4
Affiliation:
[1] Univ Sao Paulo, Inst Chem, Dept Biochem, BR-05508000 Sao Paulo, SP - Brazil
[2] Butantan Inst, Ctr Toxins Immune Response & Cell Signaling, BR-05503900 Sao Paulo, SP - Brazil
[3] Butantan Inst, Lab Cell Cycle, BR-05503900 Sao Paulo, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: Nucleic Acids Research; v. 49, n. 12, p. 7053-7074, JUL 9 2021.
Web of Science Citations: 0
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 sub-sequent 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)

FAPESP's process: 15/05776-2 - Functional characterization of Nop53/PICT1: modulation of ribosome biogenesis, the exosome activity, and effect on cell cycle
Grantee:Felipe Franco de Melo Bagatelli
Support Opportunities: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 15/06477-9 - Functional study of the components of the Saccharomyces cerevisiae exosome and the spliceosome, and their role in posttranscriptional control of gene expression
Grantee:Carla Columbano de Oliveira
Support Opportunities: Research Projects - Thematic Grants
FAPESP's process: 13/07467-1 - CeTICS - Center of Toxins, Immune-Response and Cell Signaling
Grantee:Hugo Aguirre Armelin
Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC