Study of the protein eIF5A in the translation elongation: analysis of the functional interaction with the alanine tRNA in yeast

• Grant number: 12/23396-4
• Support Opportunities: Scholarships abroad - Research Internship - Doctorate (Direct)
• Start date: April 22, 2013
• End date: April 21, 2014
• Field of knowledge: Biological Sciences - Genetics - Molecular Genetics and Genetics of Microorganisms
• Principal Investigator: Cleslei Fernando Zanelli
• Grantee: Tatiana Faria Watanabe
• Supervisor: Jonathan D. Dinman
• Host Institution: Faculdade de Ciências Farmacêuticas (FCFAR). Universidade Estadual Paulista (UNESP). Campus de Araraquara. Araraquara , SP, Brazil
• Institution abroad: University of Maryland, College Park, United States

Abstract

eIF5A is a protein essential for cell viability, highly conserved in eukaryotes and archaea presents a post-translational modification where only a specific residue of lysine is modified to the amino acid hipusina. The process named hipusinação is essential for the function of eIF5A and thus for cell viability. eIF5A was initially described as a translation initiation factor because it stimulates the synthesis of methionyl-puromycin in vitro, but recent data from our and other laboratories have shown a role for eIF5A in the elongation step. eIF5A has a structural homolog, the translation elongation factor P (EF-P) of bacteria. EF-P stimulates the synthesis of methionyl-puromycin and is essential for cell viability in bacteria. Functional studies suggest that EF-P preferentially stimulates the formation of peptide bonds amino acid side chain short. Looking for other cellular factors that could improve growth of eIF5A temperature-sensitive mutants when overexpressed, we found the tRNA for alanine (tRNAAla), this data suggest that a possible functional correlation between these factors. Given the structural homology between eIF5A and EF-P and possible functional homology, it is intended to understand the relationship of eIF5A with alanine tRNA and thus contribute to the characterization of the specific role of this protein in the translation elongation. (AU)