Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae - PubMed (original) (raw)
. 1994 Feb 11;269(6):3934-40.
Affiliations
- PMID: 8307948
Free article
Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae
H A Kang et al. J Biol Chem. 1994.
Free article
Abstract
Eukaryotic translation initiation factor eIF-5A (formerly eIF-4D) is thought to function in protein synthesis by promoting synthesis of the first peptide bond because it stimulates methionyl-puromycin formation in vitro. eIF-5A is encoded by two genes (TIF51A and TIF51B) in Saccharomyces cerevisiae; the protein and its hypusine modification are essential for cell viability. To analyze the factor's function in vivo, we expressed from the repressible GAL promoter a functional but unstable eIF-5A fusion protein (R-eIF-5A) with an NH2-terminal arginine which is subject to rapid turnover through the NH2-terminal end rule proteolytic pathway. When the conditional mutant strain is shifted from galactose to glucose medium, the rapid disappearance of R-eIF-5A protein occurs within one generation, causing an immediate inhibition of cell growth. However, eIF-5A-depleted cells synthesize protein at about 70% of the wild type rate and exhibit only a slight change in polysome profiles reflecting a subtle defect in a late step of translation initiation. These results suggest that the activity of eIF-5A may not be absolutely essential for general protein synthesis. Rather, eIF-5A may be selectively required for translation of certain mRNAs and/or may be involved in some other aspect of cell metabolism.
Similar articles
- Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae.
Schnier J, Schwelberger HG, Smit-McBride Z, Kang HA, Hershey JW. Schnier J, et al. Mol Cell Biol. 1991 Jun;11(6):3105-14. doi: 10.1128/mcb.11.6.3105-3114.1991. Mol Cell Biol. 1991. PMID: 1903841 Free PMC article. - Translation initiation factor eIF-5A, the hypusine-containing protein, is phosphorylated on serine in Saccharomyces cerevisiae.
Kang HA, Schwelberger HG, Hershey JW. Kang HA, et al. J Biol Chem. 1993 Jul 15;268(20):14750-6. J Biol Chem. 1993. PMID: 8325852 - Eukaryotic initiation factor 5A activity and HIV-1 Rev function.
Bevec D, Hauber J. Bevec D, et al. Biol Signals. 1997 May-Jun;6(3):124-33. doi: 10.1159/000109118. Biol Signals. 1997. PMID: 9285095 Review.
Cited by
- Changes in a Protein Profile Can Account for the Altered Phenotype of the Yeast Saccharomyces cerevisiae Mutant Lacking the Copper-Zinc Superoxide Dismutase.
Kwolek-Mirek M, Dubicka-Lisowska A, Bednarska S, Zadrag-Tecza R, Kaszycki P. Kwolek-Mirek M, et al. Metabolites. 2023 Mar 22;13(3):459. doi: 10.3390/metabo13030459. Metabolites. 2023. PMID: 36984899 Free PMC article. - Translation factor eIF5a is essential for IFNγ production and cell cycle regulation in primary CD8+ T lymphocytes.
Tan TCJ, Kelly V, Zou X, Wright D, Ly T, Zamoyska R. Tan TCJ, et al. Nat Commun. 2022 Dec 17;13(1):7796. doi: 10.1038/s41467-022-35252-y. Nat Commun. 2022. PMID: 36528626 Free PMC article. - eIF5A is activated by virus infection or dsRNA and facilitates virus replication through modulation of interferon production.
Seoane R, Llamas-González YY, Vidal S, El Motiam A, Bouzaher YH, Fonseca D, Farrás R, García-Sastre A, González-Santamaría J, Rivas C. Seoane R, et al. Front Cell Infect Microbiol. 2022 Jul 27;12:960138. doi: 10.3389/fcimb.2022.960138. eCollection 2022. Front Cell Infect Microbiol. 2022. PMID: 35967877 Free PMC article. - The eukaryotic initiation factor 5A (eIF5A1), the molecule, mechanisms and recent insights into the pathophysiological roles.
Tauc M, Cougnon M, Carcy R, Melis N, Hauet T, Pellerin L, Blondeau N, Pisani DF. Tauc M, et al. Cell Biosci. 2021 Dec 24;11(1):219. doi: 10.1186/s13578-021-00733-y. Cell Biosci. 2021. PMID: 34952646 Free PMC article. Review. - Integrated Multi-Omics Analysis of Mechanisms Underlying Yeast Ethanol Tolerance.
Šoštarić N, Arslan A, Carvalho B, Plech M, Voordeckers K, Verstrepen KJ, van Noort V. Šoštarić N, et al. J Proteome Res. 2021 Aug 6;20(8):3840-3852. doi: 10.1021/acs.jproteome.1c00139. Epub 2021 Jul 8. J Proteome Res. 2021. PMID: 34236875 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases