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J Biol Chem, Vol. 273, Issue 32, 20404-20416, August 7, 1998
From the Based on characteristic amino acid sequences of
kinases that phosphorylate the
cpc-3, the Neurospora crassa Homologue of
Yeast GCN2, Encodes a Polypeptide with Juxtaposed
eIF2
Kinase and Histidyl-tRNA Synthetase-related Domains
Required for General Amino Acid Control
§,
Institute of Applied Genetics, University of
Hannover, Herrenhäuser Strasse 2, D-30419 Hannover, Germany
and the § Laboratory of Eukaryotic Gene Regulation, NICHD,
National Institutes of Health, Bethesda, Maryland 20892-2716
subunit of eukaryotic translation
initiation factor 2 (eIF2 kinases), degenerate oligonucleotide
primers were constructed and used to polymerase chain reaction-amplify
from genomic DNA of Neurospora crassa a sequence encoding
part of a putative protein kinase. With this sequence an open reading
frame was identified encoding a predicted polypeptide with juxtaposed eIF2 kinase and histidyl-tRNA synthetase-related domains. The 1646 amino acid sequence of this gene, called cpc-3, showed 35% positional identity over almost the entire sequence with GCN2 of yeast,
which stimulates translation of the transcriptional activator of amino
acid biosynthetic genes encoded by GCN4. Strains disrupted
for cpc-3 were unable to induce increased transcription and
derepression of amino acid biosynthetic enzymes in amino acid-deprived cells. The cpc-3 mutation did not affect the ability to
up-regulate mRNA levels of cpc-1, encoding the
GCN4 homologue and transcriptional activator of amino acid
biosynthetic genes in N. crassa, but the mutation abolished
the dramatic increase of CPC1 protein level in response to amino acid
deprivation. These findings suggest that cpc-3 is the
functional homologue of GCN2, being required for increased
translation of cpc-1 mRNA in amino acid-starved cells.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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