Advanced search
Start date

Study of the role of elF5A in translation elongation

Grant number: 10/50044-6
Support type:Research Projects - Thematic Grants
Duration: July 01, 2010 - February 29, 2016
Field of knowledge:Biological Sciences - Biochemistry - Molecular Biology
Principal researcher:Sandro Roberto Valentini
Grantee:Sandro Roberto Valentini
Home Institution: Faculdade de Ciências Farmacêuticas (FCFAR). Universidade Estadual Paulista (UNESP). Campus de Araraquara. Araraquara , SP, Brazil
Associated grant(s):13/13225-0 - YEAST 2013: 26th International Conference on Yeast Genetics and Molecular Biology, AR.EXT
Associated scholarship(s):15/07728-5 - Analysis of the functional relationship between eIF5A and the transcription factor Hac1 in Saccharomyces cerevisiae, BP.MS
15/01938-8 - Translation profile of eIF5A dys1-1 hypusination mutant, BP.PD
14/22067-2 - GC7 hypusination inhibitor specificity and toxicity study using Saccharomyces cerevisiae model, BP.IC
+ associated scholarships 14/06270-2 - A specificity and toxicity study of GC7 hypusination inhibitor using Saccharomyces cerevisiae model, BP.IC
13/10888-9 - Generation and production of single-cysteine mutants of human eIF5A-2 to be used on ribosome binding assays, BP.IC
13/02233-2 - Study of the role of protein eIF5A in specific tranlation using the model Saccharomyces cerevisiae, BP.MS
13/06939-7 - Generation of new mutants of eIF5A protein using the strategy of alanine scanning, BP.IC
12/23890-9 - Biochemical and kinetic study of eIF5A and ribosome direct interaction, using Saccharomyces cerevisiae and human as models, BP.PD
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 - associated scholarships


The translation initiation factor 5A (eIF5A) is highly conserved from archaea to mammals and essential for cell viability. eIF5A is the only protein known to contain the essential amino acid residue hypusine, generated by the enzymes deoxyhypusine synthase and deoxyhypusine hydroxylase. Recent results obtained in our previous study strongly suggest that eIF5A has a role in translation elongation. Therefore, in this project we intend to further investigate the role of eIF5A in translation using the following experimental proposals: 1) study of the functional interaction between eIF5A and translation elongation factors; 2) mapping of eIF5A ribosome binding sites using directed hydroxyl radical probing of rRNA; 3) investigation of a possible role for eIF5A in translation termination; 4) analysis of the functional relationship between eIF5A and tRNAAla; 5) analysis of the association of eIF5A with the secretory pathway and the control of gene expression at the translational level; 6) functional study of the enzyme deoxyhypusine synthase, involved in the first step of eIF5A hypusination; 7) analysis of genetic interactions in large scale involving eIF5A using the Synthetic Genetic Array Analysis - SGA. We expect that the results of these approaches not only unveil additional information on the role played by eIF5A in translation but also determine its involvement in the control of gene expression at the translational level. (AU)

Articles published in Agência FAPESP Newsletter about the research grant:
Pós-doutorado em biologia molecular com Bolsa da FAPESP 

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)
ROSSI, DANUZA; BARBOSA, NATALIA M.; GALVAO, FABIO C.; BOLDRIN, PAULO E. G.; HERSHEY, JOHN W. B.; ZANELLI, CLESLEI F.; FRASER, CHRISTOPHER S.; VALENTINI, SANDRO R. Evidence for a Negative Cooperativity between eIF5A and eEF2 on Binding to the Ribosome. PLoS One, v. 11, n. 4 APR 26 2016. Web of Science Citations: 4.
BRANTIS-DE-CARVALHO, CARLOS EDUARDO; MAARIFI, GHIZLANE; GONCALVES BOLDRIN, PAULO EDUARDO; ZANELLI, CLESLEI FERNANDO; NISOLE, SEBASTIEN; CHELBI-ALIX, MOUNIRA K.; VALENTINI, SANDRO ROBERTO. MxA interacts with and is modified by the SUMOylation machinery. Experimental Cell Research, v. 330, n. 1, p. 151-163, JAN 1 2015. Web of Science Citations: 9.

Please report errors in scientific publications list by writing to: