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Genetics

Title:		Fertility and polarized cell growth depends on eIF5A for translation of polyproline-rich formins in Saccharomyces cerevisiae
Author(s):		Li T; Belda-Palazon B; Ferrando A; Alepuz P;
Address:		"Departamento de Bioquimica y Biologia Molecular, Facultad de Ciencias Biologicas, Universitat de Valencia, E-46100 Burjassot, Valencia, Spain. Instituto de Biologia Molecular y Celular de Plantas, Centro Superior de Investigaciones Cientificas-Universidad Politecnica de Valencia, 46022 Valencia, Spain. Instituto de Biologia Molecular y Celular de Plantas, Centro Superior de Investigaciones Cientificas-Universidad Politecnica de Valencia, 46022 Valencia, Spain paula.alepuz@uv.es aferrando@ibmcp.upv.es. Departamento de Bioquimica y Biologia Molecular, Facultad de Ciencias Biologicas, Universitat de Valencia, E-46100 Burjassot, Valencia, Spain paula.alepuz@uv.es aferrando@ibmcp.upv.es"
Journal Title:		Genetics
Year:		2014
Volume:		20140611
Issue:		4
Page Number:		1191 - 1200
DOI:		10.1534/genetics.114.166926
ISSN/ISBN:		1943-2631 (Electronic) 0016-6731 (Print) 0016-6731 (Linking)
Abstract:		"eIF5A is an essential and evolutionary conserved translation elongation factor, which has recently been proposed to be required for the translation of proteins with consecutive prolines. The binding of eIF5A to ribosomes occurs upon its activation by hypusination, a modification that requires spermidine, an essential factor for mammalian fertility that also promotes yeast mating. We show that in response to pheromone, hypusinated eIF5A is required for shmoo formation, localization of polarisome components, induction of cell fusion proteins, and actin assembly in yeast. We also show that eIF5A is required for the translation of Bni1, a proline-rich formin involved in polarized growth during shmoo formation. Our data indicate that translation of the polyproline motifs in Bni1 is eIF5A dependent and this translation dependency is lost upon deletion of the polyprolines. Moreover, an exogenous increase in Bni1 protein levels partially restores the defect in shmoo formation seen in eIF5A mutants. Overall, our results identify eIF5A as a novel and essential regulator of yeast mating through formin translation. Since eIF5A and polyproline formins are conserved across species, our results also suggest that eIF5A-dependent translation of formins could regulate polarized growth in such processes as fertility and cancer in higher eukaryotes"
Keywords:		"Actins/metabolism Cytoskeletal Proteins/genetics/metabolism Membrane Proteins/genetics/metabolism Microfilament Proteins/genetics/*metabolism Morphogenesis Mutation *Peptide Chain Elongation, Translational Peptide Initiation Factors/genetics/*metabolism P;"
Notes:		"MedlineLi, Tianlu Belda-Palazon, Borja Ferrando, Alejandro Alepuz, Paula eng Research Support, Non-U.S. Gov't 2014/06/14 Genetics. 2014 Aug; 197(4):1191-200. doi: 10.1534/genetics.114.166926. Epub 2014 Jun 11"