Casein kinase II mediates multiple phosphorylation of Saccharomyces cerevisiae eIF-2 alpha (encoded by SUI2), which is required for optimal eIF-2 function in S. cerevisiae (Q36662543)

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scientific article published on August 1994

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English	Casein kinase II mediates multiple phosphorylation of Saccharomyces cerevisiae eIF-2 alpha (encoded by SUI2), which is required for optimal eIF-2 function in S. cerevisiae	scientific article published on August 1994

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

Casein kinase II mediates multiple phosphorylation of Saccharomyces cerevisiae eIF-2 alpha (encoded by SUI2), which is required for optimal eIF-2 function in S. cerevisiae (English)

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

Saccharomyces cerevisiae

1 reference

based on heuristic

inferred from title

phosphorylation

1 reference

based on heuristic

inferred from title

author name string

L Feng

1

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

H Yoon

2

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

T F Donahue

3

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

language of work or name

0 references

publication date

1 August 1994

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

Molecular and Cellular Biology

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Europe PubMed Central

PMC publication ID

15 August 2017

14

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

8

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

5139-5153

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

A protein complex of translational regulators of GCN4 mRNA is the guanine nucleotide-exchange factor for translation initiation factor 2 in yeast

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=359033

30 September 2017

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

1 reference

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Regulation of topoisomerase II by phosphorylation: a role for casein kinase II.

1 reference

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Mutations in the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2 alpha) that overcome the inhibitory effect of eIF-2 alpha phosphorylation on translation initiation

1 reference

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Mammalian eukaryotic initiation factor 2 alpha kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast

1 reference

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30 September 2017

Positive regulation in the general amino acid control of Saccharomyces cerevisiae

1 reference

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Mechanism of translational control by partial phosphorylation of the alpha subunit of eukaryotic initiation factor 2.

1 reference

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Vector systems for the expression, analysis and cloning of DNA sequences in S. cerevisiae

1 reference

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Eukaryotic protein synthesis

1 reference

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The alpha subunit of initiation factor 2 is phosphorylated in vivo in the yeast Saccharomyces cerevisiae

1 reference

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30 September 2017

Multiple upstream AUG codons mediate translational control of GCN4.

1 reference

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Phosphorylation of the guanine nucleotide exchange factor from rabbit reticulocytes regulates its activity in polypeptide chain initiation

1 reference

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The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2

1 reference

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5-Fluoroorotic acid as a selective agent in yeast molecular genetics

1 reference

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Activation of casein kinase II in response to insulin and to epidermal growth factor

1 reference

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Isolation, sequencing, and disruption of the CKA1 gene encoding the alpha subunit of yeast casein kinase II

1 reference

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30 September 2017

Mechanisms of gene regulation in the general control of amino acid biosynthesis in Saccharomyces cerevisiae.

1 reference

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30 September 2017

Cloning and sequencing of complementary DNAs encoding the alpha-subunit of translational initiation factor eIF-2. Characterization of the protein and its messenger RNA

1 reference

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30 September 2017

Mutations in the structural genes for eukaryotic initiation factors 2 alpha and 2 beta of Saccharomyces cerevisiae disrupt translational control of GCN4 mRNA

1 reference

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Myc oncoproteins are phosphorylated by casein kinase II

1 reference

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30 September 2017

Juxtaposition of domains homologous to protein kinases and histidyl-tRNA synthetases in GCN2 protein suggests a mechanism for coupling GCN4 expression to amino acid availability

1 reference

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30 September 2017

Yeast translation initiation suppressor sui2 encodes the alpha subunit of eukaryotic initiation factor 2 and shares sequence identity with the human alpha subunit.

1 reference

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30 September 2017

The scanning model for translation: an update

1 reference

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30 September 2017

Dephosphorylation or antibody binding to the carboxy terminus stimulates pp60c-src

1 reference

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30 September 2017

Stimulation of casein kinase II by epidermal growth factor: relationship between the physiological activity of the kinase and the phosphorylation state of its beta subunit

1 reference

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30 September 2017

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.

1 reference

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Casein kinase 2: an 'eminence grise' in cellular regulation?

1 reference

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30 September 2017

Isolation, sequencing, and disruption of the yeast CKA2 gene: casein kinase II is essential for viability in Saccharomyces cerevisiae

1 reference

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

1 reference

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Genetic characterization of the Saccharomyces cerevisiae translational initiation suppressors sui1, sui2 and SUI3 and their effects on HIS4 expression

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Cloning genes by complementation in yeast

1 reference

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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

1 reference

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Translational control in mammalian cells

1 reference

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Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast

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The suil suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNA(iMet) recognition of the start codon

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Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon

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Cloning of the cDNA of the heme-regulated eukaryotic initiation factor 2 alpha (eIF-2 alpha) kinase of rabbit reticulocytes: homology to yeast GCN2 protein kinase and human double-stranded-RNA-dependent eIF-2 alpha kinase

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1 reference

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Casein kinase II phosphorylates p34cdc2 kinase in G1 phase of the HeLa cell division cycle

1 reference

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Human p68 kinase exhibits growth suppression in yeast and homology to the translational regulator GCN2

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Truncated protein phosphatase GLC7 restores translational activation of GCN4 expression in yeast mutants defective for the eIF-2 alpha kinase GCN2

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Casein kinase II phosphorylates the eukaryote-specific C-terminal domain of topoisomerase II in vivo

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Mutation analysis of the Cys-X2-Cys-X19-Cys-X2-Cys motif in the beta subunit of eukaryotic translation initiation factor 2

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Purification of the eukaryotic initiation factor 2-eukaryotic initiation factor 2B complex and characterization of its guanine nucleotide exchange activity during protein synthesis initiation

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Genetic applications of yeast transformation with linear and gapped plasmids

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Oligonucleotide-Directed Mutagenesis: A Simple Method Using Two Oligonucleotide Primers and a Single-Stranded DNA Template

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Structural studies on the eukaryotic chain initiation factor 2 from rabbit reticulocytes and brine shrimp Artemia embryos. Phosphorylation by the heme-controlled repressor and casein kinase II

1 reference

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Identifiers

10.1128/MCB.14.8.5139

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 August 2017

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