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Posttranscriptional control of gene expression: pre-rRNA processing, mRNA degradation, splicing and snoRNP assembly in Saccharomyces cerevisiae

Grant number: 20/00901-1
Support Opportunities:Research Projects - Thematic Grants
Duration: July 01, 2021 - June 30, 2026
Field of knowledge:Biological Sciences - Biochemistry - Molecular Biology
Principal Investigator:Carla Columbano de Oliveira
Grantee:Carla Columbano de Oliveira
Host Institution: Instituto de Química (IQ). Universidade de São Paulo (USP). São Paulo , SP, Brazil
Associated researchers:Alexander Henning Ulrich ; Marcos Vicente de Albuquerque Salles Navarro ; Olivier Gadal
Associated grant(s):23/00368-0 - Use of High Resolution Microscopy to Investigate the Functional Role of the Exosome in Sub-Nucleolar Complexes, AP.R SPRINT
22/08812-3 - Multi-user equipment approved in the project 20/00901-1: liquid chromatography system FPLC, AP.EMU
Associated scholarship(s):24/02036-7 - Characterization of the role of the exoxome subunity DIS3 in the control of cell cycle, BP.PD
23/06344-5 - Analysis of the effect of the presence of 7S pre-rRNA on 60S subunits on translation in S. cerevisiae, BP.DR
22/16359-7 - Interaction characterization of new proteins with the exosome, BP.IC
+ associated scholarships 22/06549-3 - Effect of The Absence of The Splicing Factor Cwc24 on Prp11 Interactome in Saccharomyces cerevisiae, BP.IC
22/00071-4 - Identification of karyopherins involved in the nuclear import of exosome subunits in Saccharomyces cerevisiae, BP.PD
21/14620-7 - Influence of the phosphorylation of proteins from the 90s preribosome complex on the recruitment of exosome and its role in signaling during the processing and quality control of pre-rRNAS, BP.PD
21/14137-4 - Characterization of the role to the general splicing-factor CWC24 in pre-mRNA in Saccharomyces cerevisiae, BP.DD - associated scholarships

Abstract

In eukaryotes, RNAs undergo many processing steps before becoming functional; these steps require specific protein-protein and protein-RNA interactions that are essential for the control of gene expression. We have characterized the function of various yeast proteins, involved in different steps of RNA processing. The RNase named exosome has been the main focus of the research in my group, studying the function of the yeast exosome and the structure of the yeast and archaeal exosome. With this project we propose to continue studying the exosome, mainly the subcellular localization of its subunits and the recruitment of the complex to pre-ribosomal particles. A new challenge is also proposed, that of the study the role of the exosome in mRNA degradation in human cells. We also intend to continue studying Saccharomyces cerevisiae proteins that have been first identified and characterized in our lab, which are involved in various steps of control of gene expression, interconnected by protein interactions. Nop17 is at the center of these interactions, and as a subunit of the co-chaperone complex R2TP, participates in the assembly of multisubunit complexes. Nop17 interacts with the exosome, with splicing factors, snoRNP subunits, pre-60S proteins, and with a protein containing Fe/S clusters. This project is therefore very broad and involves the study of different enzymatic complexes. Given the evolutionary conservation of these processes in eukaryotes, the results obtained here may be later extrapolated to human cells. Importantly, mutations in the genes of orthologs of the proteins studied by us are known to be associated with human genetic diseases. (AU)

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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
CARVALHO, FELIPE A.; MUEHLENHOFF, ULRICH; BRAYMER, JOSEPH J.; ROOT, VASILIJ; STUEMPFIG, MARTIN; OLIVEIRA, CARLA C.; LILL, ROLAND. Hsp90 and metal-binding J-protein family chaperones are not critically involved in cellular iron-sulfur protein assembly and iron regulation in yeast. FEBS Letters, v. 597, n. 13, p. 15-pg., . (19/00527-5, 20/00901-1, 21/06497-0)

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