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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 controls association of the RNA exosome with pre-60S particles in yeast

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Author(s):
Cepeda, Leidy Paola P. [1] ; Bagatelli, Felipe F. M. [1] ; Santos, Renata M. [2] ; Santos, Marlon D. M. [3] ; Nogueira, Fabio C. S. [2, 4] ; Oliveira, Carla C. [1]
Total Authors: 6
Affiliation:
[1] Univ Sao Paulo, Inst Chem, Dept Biochem, BR-05508000 Sao Paulo, SP - Brazil
[2] Univ Fed Rio de Janeiro, Prote Unit, Rio de Janeiro, RJ - Brazil
[3] Fiocruz MS, Carlos Chagas Inst, Lab Struct & Computat Prote, Curitiba, PR - Brazil
[4] Univ Fed Rio de Janeiro, LADETEC, Lab Prote, Rio de Janeiro, RJ - Brazil
Total Affiliations: 4
Document type: Journal article
Source: Journal of Biological Chemistry; v. 294, n. 50, p. 19365+, DEC 13 2019.
Web of Science Citations: 0
Abstract

Eukaryotic ribosomal biogenesis is a highly energy-demanding and complex process that requires hundreds of trans-acting factors to dynamically build the highly organized 40S and 60S subunits. Each ribonucleoprotein complex comprises specific rRNAs and ribosomal proteins that are organized into functional domains. The RNA exosome complex plays a crucial role as one of the pre-60S-processing factors, because it is the RNase responsible for processing the 7S pre-rRNA to the mature 5.8S rRNA. The yeast pre-60S assembly factor Nop53 has previously been shown to associate with the nucleoplasmic pre-60S in a region containing the ``foot{''} structure assembled around the 3' end of the 7S pre-rRNA. Nop53 interacts with 25S rRNA and with several 60S assembly factors, including the RNA exosome, specifically, with its catalytic subunit Rrp6 and with the exosome-associated RNA helicase Mtr4. Nop53 is therefore considered the adaptor responsible for recruiting the exosome complex for 7S processing. Here, using proteomics-based approaches in budding yeast to analyze the effects of Nop53 on the exosome interactome, we found that the exosome binds pre-ribosomal complexes early during the ribosome maturation pathway. We also identified interactions through which Nop53 modulates exosome activity in the context of 60S maturation and provide evidence that in addition to recruiting the exosome, Nop53 may also be important for positioning the exosome during 7S processing. On the basis of these findings, we propose that the exosome is recruited much earlier during ribosome assembly than previously thought, suggesting the existence of additional interactions that remain to be described. (AU)

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: 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)