Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2. (Q27935862)

Journal of Biological Chemistry

GOA release 2020-03-11

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S Zhu

1

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A Y Sobolev

series ordinal

2

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R C Wek

series ordinal

3

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language of work or name

English

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publication date

4 October 1996

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published in

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1 December 2016

271

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issue

40

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page(s)

24989-94

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cites work

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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 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

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Structural and functional relationships between aminoacyl-tRNA synthetases

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

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

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The highly acidic C-terminal region of the yeast initiation factor subunit 2 alpha (eIF-2 alpha) contains casein kinase phosphorylation sites and is essential for maintaining normal regulation of GCN4.

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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

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