Mutations Activating theYeasteIF-2o Kinase GCN2: Isolation ofAlleles Altering theDomainRelated to Histidyl-tRNA Synthetases (original) (raw)

Mutations activating the yeast eIF-2 alpha kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases

Belinda Jackson

Molecular and Cellular Biology, 1992

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The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids

Shuhao Zhu

Molecular and cellular biology, 1995

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The tRNA-binding moiety in GCN2 contains a dimerization domain that interacts with the kinase domain and is required for tRNA binding and kinase activation

Alan Hinnebusch

The EMBO Journal, 2001

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Defects in tRNA processing and nuclear export induce GCN4 translation independently of phosphorylation of the alpha subunit of eukaryotic translation initiation factor …

A. Hopper

… and cellular biology, 2000

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Interplay between GCN2 and GCN4 expression, translation elongation factor 1 mutations and translational fidelity in yeast

Alan Hinnebusch

Nucleic Acids Research, 2005

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Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of eIF2alpha kinase GCN2

Hongfang Qiu

Molecular and cellular biology, 1997

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Suppression of ribosomal reinitiation at upstream open reading frames in amino acid-starved cells forms the basis for GCN4 translational control

Belinda Jackson

Molecular and Cellular Biology, 1991

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Genetic evidence for functional specificity of the yeast GCN2 kinase

Nektarios Tavernarakis

MGG Molecular & General Genetics, 1996

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Histidyl-tRNA Synthetase-related Sequences in GCN2 Protein Kinase Regulate in Vitro Phosphorylation of eIF-2

Alexander Sobolev

Journal of Biological Chemistry, 1996

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Interaction between the tRNA-Binding and C-Terminal Domains of Yeast Gcn2 Regulates Kinase Activity In Vivo

Mark Ashe

PLOS Genetics, 2015

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Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2

Hongfang Qiu

Genes & Development, 2002

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Gene overexpression reveals alternative mechanisms that induce GCN4 mRNA translation

Nektarios Tavernarakis

Gene, 1996

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Evidence that GCD6 and GCD7, translational regulators of GCN4, are subunits of the guanine nucleotide exchange factor for eIF-2 in Saccharomyces cerevisiae

Robert Matts

Molecular and Cellular Biology, 1993

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Minimum Requirements for the Function of Eukaryotic Translation Initiation Factor 2

Joseph Nika

2000

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Uncharged tRNA Activates GCN2 by Displacing the Protein Kinase Moiety from a Bipartite tRNA-Binding Domain

Alan Hinnebusch

Molecular Cell, 2000

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Snf1 Promotes Phosphorylation of the Subunit of Eukaryotic Translation Initiation Factor 2 by Activating Gcn2 and Inhibiting Phosphatases Glc7 and Sit4

Hongfang Qiu, Vera Cherkasova

Molecular and Cellular Biology, 2010

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Regulation of internal ribosome entry site-mediated translation by eukaryotic initiation factor-2α phosphorylation and translation of a small upstream open reading …

Maria Hatzoglou

Journal of Biological …, 2002

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Increased tRNA level in yeast cells with mutant translation termination factors eRF1 and eRF3

S. Inge-vechtomov

Molecular Biology, 2006

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The molecular aetiology of tRNA synthetase depletion: induction of aGCN4amino acid starvation response despite homeostatic maintenance of charged tRNA levels

Brandon Childers

2019

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Increased tRNA level in yeast cells with mutant translation termination factors eRF1 and eRF

Galina Zhouravleva

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Dominant-negative mutant phenotypes and the regulation of translation elongation factor 2 levels in yeast

Dominic Ortiz

Nucleic Acids Research, 2005

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Identification of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expression

Belinda Jackson

Molecular and Cellular Biology, 1990

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GCD10, a translational repressor of GCN4, is the RNA-binding subunit of eukaryotic translation initiation factor-3

Mercedes Tamame

Genes & Development, 1995

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5'TRU: Identification and Analysis of Translationally Regulative 5'Untranslated Regions in Amino Acid Starved Yeast Cells

Burkhard Morgenstern

Molecular & Cellular Proteomics, 2011

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Eukaryotic Translation Initiation Factor 4E-Dependent Translation Is Not Essential for Survival of Starved Yeast Cells

Mordechai Choder

Journal of Bacteriology, 2001

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Global translational impacts of the loss of the tRNA modification t6A in yeast

Alvaro Glavic

Microbial Cell, 2016

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Guanine Nucleotide Pool Imbalance Impairs Multiple Steps of Protein Synthesis and Disrupts GCN4 Translational Control in Saccharomyces cerevisiae

Mercedes Tamame

Genetics, 2011

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[Increased tRNA concentration in yeast containing mutant termination translation factors eRF1 and eRF3]

Galina Zhouravleva

Molekuliarnaia biologiia

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Crystal Structures of GCN2 Protein Kinase C-terminal Domains Suggest Regulatory Differences in Yeast and Mammals

Isha Singh

Journal of Biological Chemistry, 2014

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Guanine Nucleotide Pool Imbalance Impairs Multiple Steps of Protein Synthesis and Disrupts GCN4 Translational Control in Saccharomyces cerevisiae

Mercedes Tamame

Genetics, 2011

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Genome-wide Analysis of tRNA Charging and Activation of the eIF2 Kinase Gcn2p

Florian Freimoser

Journal of Biological Chemistry, 2009

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Repression of GCN4 mRNA Translation by Nitrogen Starvation in Saccharomyces cerevisiae

Gerhard Braus

Journal of Biological Chemistry, 2001

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Charcot–Marie–Tooth mutation in glycyl-tRNA synthetase stalls ribosomes in a pre-accommodation state and activates integrated stress response

samantha mendonsa

Nucleic Acids Research, 2021

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The A1 x U72 base pair conserved in eukaryotic initiator tRNAs is important specifically for binding to the eukaryotic translation initiation factor eIF2

Uttam Rajbhandary

Molecular and Cellular Biology, 1996

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Tight Binding of the Phosphorylated α Subunit of Initiation Factor 2 (eIF2α) to the Regulatory Subunits of Guanine Nucleotide Exchange Factor eIF2B Is Required for Inhibition of Translation Initiation

Graham Pavitt

Molecular and Cellular Biology, 2001

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