title: The eEF1γ subunit contacts RNA polymerase II and binds vimentin promoter region.
abstract: Here, we show that the eukaryotic translation elongation factor 1 gamma (eEF1γ) physically interacts with the RNA polymerase II (pol II) core subunit 3 (RPB3), both in isolation and in the context of the holo-enzyme. Importantly, eEF1γ has been recently shown to bind Vimentin mRNA. By chromatin immunoprecipitation experiments, we demonstrate, for the first time, that eEF1γ is also physically present on the genomic locus corresponding to the promoter region of human Vimentin gene. The eEF1γ depletion causes the Vimentin protein to be incorrectly compartmentalised and to severely compromise cellular shape and mitochondria localisation. We demonstrate that eEF1γ partially colocalises with the mitochondrial marker Tom20 and that eEF1γ depletion increases mitochondrial superoxide generation as well as the total levels of carbonylated proteins. Finally, we hypothesise that eEF1γ, in addition to its role in translation elongation complex, is involved in regulating Vimentin gene by contacting both pol II and the Vimentin promoter region and then shuttling/nursing the Vimentin mRNA from its gene locus to its appropriate cellular compartment for translation.
authors.affiliation: Istituto di Biologia e Patologia Molecolari CNR, c/o Regina Elena Cancer Institute, Rome, Italy.
authors.forename: Nicoletta
authors.initials: N
authors.lastname: Corbi
authors.forename: Enrico Maria
authors.initials: EM
authors.lastname: Batassa
authors.forename: Cinzia
authors.initials: C
authors.lastname: Pisani
authors.forename: Annalisa
authors.initials: A
authors.lastname: Onori
authors.forename: Maria Grazia
authors.initials: MG
authors.lastname: Di Certo
authors.forename: Georgios
authors.initials: G
authors.lastname: Strimpakos
authors.forename: Maurizio
authors.initials: M
authors.lastname: Fanciulli
authors.forename: Elisabetta
authors.initials: E
authors.lastname: Mattei
authors.forename: Claudio
authors.initials: C
authors.lastname: Passananti
mesh_terms: D002244:Carbon / Q000737:chemistry; D005136:Eye Proteins / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D026901:Membrane Transport Proteins / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D000090622:Mitochondrial Precursor Protein Import Complex Proteins; D024101:Mitochondrial Proteins / Q000378:metabolism; D020648:Peptide Elongation Factor 1 / Q000235:genetics* / Q000378:metabolism; D011401:Promoter Regions, Genetic; D011485:Protein Binding; D014176:Protein Biosynthesis; D017434:Protein Structure, Tertiary; D012319:RNA Polymerase II / Q000235:genetics* / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000378:metabolism; D012177:Retinol-Binding Proteins / Q000378:metabolism; D013481:Superoxides / Q000378:metabolism; D020798:Two-Hybrid System Techniques; D014746:Vimentin / Q000235:genetics*; D000099214:Retinol-Binding Proteins, Interstitial
chemical_list: D002244:Carbon; D005136:Eye Proteins; D026901:Membrane Transport Proteins; D000090622:Mitochondrial Precursor Protein Import Complex Proteins; D024101:Mitochondrial Proteins; D020648:Peptide Elongation Factor 1; D012319:RNA Polymerase II; D011956:Receptors, Cell Surface; D012177:Retinol-Binding Proteins; D013481:Superoxides; D014746:Vimentin; D000099214:Retinol-Binding Proteins, Interstitial; C084008:TOMM20 protein, human