Literature DB >> 17179749

The translation elongation factor eEF1B plays a role in the oxidative stress response pathway.

Olubunmi Olarewaju1, Pedro A Ortiz, Wasimul Q Chowdhury, Ishita Chatterjee, Terri Goss Kinzy.   

Abstract

The multi-subunit guanine nucleotide exchange factor eEF1B for Saccharomyces cerevisiae Translation Elongation Factor 1A (eEF1A) has catalytic (eEF1Balpha) and noncatalytic (eEF1Bgamma) subunits. Deletion of the two nonessential genes encoding eEF1Bgamma has no dramatic effects on total protein synthesis or translational fidelity. Instead, loss of each gene gives resistance to oxidative stress, and loss of both is additive. The level of stress resistance is similar to overexpression of the Yap1p stress transcription factor and is dependent on the presence of the YAP1gene. Cells lacking the catalytic eEF1Balpha subunit show even greater resistance to CdSO(4), with or without eEF1Bgamma present. Thus, the loss of guanine nucleotide exchange activity promotes the resistance. As nucleotide exchange is a critical regulator of most G-proteins, these results indicate a new mechanism in the growing list of examples of post-transcriptional responses to cellular stress.

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Year:  2004        PMID: 17179749     DOI: 10.4161/rna.1.2.1033

Source DB:  PubMed          Journal:  RNA Biol        ISSN: 1547-6286            Impact factor:   4.652


  22 in total

1.  The eukaryotic translation elongation Factor 1Bgamma has a non-guanine nucleotide exchange factor role in protein metabolism.

Authors:  Anthony M Esposito; Terri Goss Kinzy
Journal:  J Biol Chem       Date:  2010-10-06       Impact factor: 5.157

2.  Extensive proteomic remodeling is induced by eukaryotic translation elongation factor 1Bγ deletion in Aspergillus fumigatus.

Authors:  Grainne O'Keeffe; Christoph Jöchl; Kevin Kavanagh; Sean Doyle
Journal:  Protein Sci       Date:  2013-09-30       Impact factor: 6.725

3.  Bioactivity of Cod and Chicken Protein Hydrolysates 
before and after in vitro Gastrointestinal Digestion.

Authors:  Polona Jamnik; Katja Istenič; Tatjana Koštomaj; Tune Wulff; Margrét Geirsdóttir; Annette Almgren; Rósa Jónsdóttir; Hordur G Kristinsson; Ingrid Undeland
Journal:  Food Technol Biotechnol       Date:  2017-09       Impact factor: 3.918

4.  Drosophila translational elongation factor-1gamma is modified in response to DOA kinase activity and is essential for cellular viability.

Authors:  Yujie Fan; Michael Schlierf; Ana Cuervo Gaspar; Catherine Dreux; Arlette Kpebe; Linda Chaney; Aurelie Mathieu; Christophe Hitte; Olivier Grémy; Emeline Sarot; Mark Horn; Yunlong Zhao; Terri Goss Kinzy; Leonard Rabinow
Journal:  Genetics       Date:  2009-10-19       Impact factor: 4.562

5.  Mitotic modulation of translation elongation factor 1 leads to hindered tRNA delivery to ribosomes.

Authors:  Gilad Sivan; Ranen Aviner; Orna Elroy-Stein
Journal:  J Biol Chem       Date:  2011-06-10       Impact factor: 5.157

Review 6.  The many roles of the eukaryotic elongation factor 1 complex.

Authors:  Arjun N Sasikumar; Winder B Perez; Terri Goss Kinzy
Journal:  Wiley Interdiscip Rev RNA       Date:  2012-05-03       Impact factor: 9.957

7.  Translational repression by RNA-binding protein TIAR.

Authors:  Krystyna Mazan-Mamczarz; Ashish Lal; Jennifer L Martindale; Tomoko Kawai; Myriam Gorospe
Journal:  Mol Cell Biol       Date:  2006-04       Impact factor: 4.272

8.  Targeting eEF1A by a Legionella pneumophila effector leads to inhibition of protein synthesis and induction of host stress response.

Authors:  Xihui Shen; Simran Banga; Yancheng Liu; Li Xu; Ping Gao; Ilya Shamovsky; Evgeny Nudler; Zhao-Qing Luo
Journal:  Cell Microbiol       Date:  2009-02-27       Impact factor: 3.715

9.  Kinetics of the interactions between yeast elongation factors 1A and 1Balpha, guanine nucleotides, and aminoacyl-tRNA.

Authors:  Kirill B Gromadski; Tobias Schümmer; Anne Strømgaard; Charlotte R Knudsen; Terri Goss Kinzy; Marina V Rodnina
Journal:  J Biol Chem       Date:  2007-10-09       Impact factor: 5.157

10.  Elongation factor 3, EF3, associates with the calcium channel Cch1 and targets Cch1 to the plasma membrane in Cryptococcus neoformans.

Authors:  Min Liu; Angie Gelli
Journal:  Eukaryot Cell       Date:  2008-05-23
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