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

doi:10.1128/mcb.10.6.2820-2831.1990

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Article

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

Molecular and cellular biology - 1 Jun 1990

Wek R C, Ramirez M, Jackson B M, Hinnebusch A G

Abstract excerpt

GCN4 is a transcriptional activator of amino acid-biosynthetic genes in the yeast Saccharomyces cerevisiae. GCN2, a translational activator of GCN4 expression, contains a domain homologous to the catalytic subunit of eucaryotic protein kinases. Substitution of a highly conserved lysine residue in the kinase domain abolished GCN2 regulatory function in vivo and its ability to autophosphorylate in vitro, indicating...

Topics

Alleles
Antigen-Antibody Complex
Codon
DNA-Binding Proteins
Fungal Proteins
Gene Expression Regulation, Fungal
Genes, Dominant
Genes, Fungal
Genes, Regulator
Mutation
Phosphoproteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Phosphorylation

Plasmids

Protein Biosynthesis

Protein Kinases

RNA, Messenger

Restriction Mapping

Saccharomyces cerevisiae

Source

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Identifiers

PMID: 2188100
DOI: 10.1128/mcb.10.6.2820-2831.1990
PMCID: PMC360643

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2188100-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Identification of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expression.PMID 2188100Read ↗

Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2.Semantic proximity Read ↗

Interaction between the tRNA-binding and C-terminal domains of Yeast Gcn2 regulates kinase activity in vivo.Semantic proximity Read ↗

GCN1, a translational activator of GCN4 in Saccharomyces cerevisiae, is required for phosphorylation of eukaryotic translation initiation factor 2 by protein kinase GCN2.Semantic proximity Read ↗

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

Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2.Semantic proximity Read ↗

Association of GCN1-GCN20 regulatory complex with the N-terminus of eIF2alpha kinase GCN2 is required for GCN2 activation.Semantic proximity Read ↗

The translational activator GCN3 functions downstream from GCN1 and GCN2 in the regulatory pathway that couples GCN4 expression to amino acid availability in Saccharomyces cerevisiae.Semantic proximity Read ↗

Genetic and biochemical evidence for yeast GCN2 protein kinase polymerization.Semantic proximity Read ↗

Crystal structures of GCN2 protein kinase C-terminal domains suggest regulatory differences in yeast and mammals.Semantic proximity Read ↗

Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are required for GCN2 activation in amino acid-starved cells.Semantic proximity Read ↗

Overexpression of eukaryotic translation elongation factor 3 impairs Gcn2 protein activation.Semantic proximity Read ↗

YIH1 is an actin-binding protein that inhibits protein kinase GCN2 and impairs general amino acid control when overexpressed.Semantic proximity Read ↗

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