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Biochemical and kinetic studies of yeast and human eIF5A direct binding to the ribosome

Grant number: 13/16744-9
Support Opportunities:Scholarships abroad - Research Internship - Post-doctor
Effective date (Start): December 01, 2013
Effective date (End): November 30, 2014
Field of knowledge:Biological Sciences - Biochemistry - Molecular Biology
Principal Investigator:Sandro Roberto Valentini
Grantee:Danuza Rossi
Supervisor: Christopher S. Fraser
Host Institution: Faculdade de Ciências Farmacêuticas (FCFAR). Universidade Estadual Paulista (UNESP). Campus de Araraquara. Araraquara , SP, Brazil
Research place: University of California, Davis (UC Davis), United States  
Associated to the scholarship:12/23890-9 - Biochemical and kinetic study of eIF5A and ribosome direct interaction, using Saccharomyces cerevisiae and human as models, BP.PD

Abstract

The translation factor 5A (eIF5A) is highly conserved in Archaea and eukaryotes and is essential for cell viability. This is the only protein known to contain the amino acid residue hypusine, essential for eIF5A function, generated by a post-translational modification. Although eIF5A has been extensively involved in several cellular processes, it was only recently determined a role for eIF5A in protein synthesis, more specifically in the elongation cycles. This factor enhances the peptide bond formation of specific amino acid sequences. To improve the description and understanding of the mechanism of eIF5A in translation, it is necessary to determine exactly which ribosomal complexes eIF5A binds to and the points of interaction. Two biochemical and molecular biology approaches will be used to clarify the role played by eIF5A in the translational control: 1) determination of which ribosomal complexes eIF5A binds to and the search for competitor or helper components to this binding, using fluorescence anisotropy assays; 2) identification of proteins and rRNA that physically interact with eIF5A through induction of in vitro crosslinking. The results of these goals will reveal how and where eIF5A binds to the ribosome, improving significantly the description of the role of this protein in translation. (AU)

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