Analysis of interaction between the translation factor eIF5A and components of the Ribosome quality control (RQC) complex

• Grant number: 13/25261-1
• Support Opportunities: Scholarships abroad - Research Internship - Doctorate (Direct)
• Start date: April 10, 2014
• End date: December 09, 2014
• Field of knowledge: Biological Sciences - Biochemistry - Molecular Biology
• Principal Investigator: Sandro Roberto Valentini
• Grantee: Paulo Eduardo Gonçalves Boldrin
• Supervisor: Claudio A. P. Joazeiro
• Host Institution: Faculdade de Ciências Farmacêuticas (FCFAR). Universidade Estadual Paulista (UNESP). Campus de Araraquara. Araraquara , SP, Brazil
• Institution abroad: Scripps Research Institute, San Diego, United States
• Associated to the scholarship: 12/02305-0 - Study of the physical and functional interactions between eIF5A and the translation machinery using Saccharomyces cerevisiae as a model organismo, BP.DD

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 is now clear that this factor plays a role in protein synthesis, more specifically in the elongation step. This factor enhances the peptide bond formation of specific amino acid sequences that cause ribosome stalling. Ribosome quality control (RQC) is a protein complex recruited when there is a ribosome stalling, leading to nascent peptide cleavage and ribosome recycling. Therefore, through genetic and physical interaction approaches, we intend to analyze if there is any relationship between eIF5A and factors involved in the RQC (AU)