Functional analysis of homologs of translation initiation factor 2gamma in yeast

The gamma subunit of eukaryotic translation initiation factor 2 is an EF-Tu-like protein that plays an essential role in protein synthesis. We have isolated an eIF-2gamma homolog from the fission yeast Schizosaccharomyces pombe that complements a gcd11 null allele in Saccharomyces cerevisiae. GCD11...

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Bibliographic Details
Published in:Molecular & general genetics 1997-02, Vol.253 (6), p.711-719
Main Authors: Erickson, F.L, Harding, L.D, Dorris, D.R, Hannig, E.M
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Binding Sites
BIOSINTESIS
BIOSYNTHESE
BIOSYNTHESIS
Cysteine - physiology
DNA, Complementary - isolation & purification
DNA-Binding Proteins
Drosophila
EIF-2
Eukaryotic Initiation Factor-2 - chemistry
Eukaryotic Initiation Factor-2 - genetics
Eukaryotic Initiation Factor-2 - isolation & purification
Eukaryotic Initiation Factor-2 - physiology
EXPRESION GENICA
EXPRESSION DES GENES
Fungal Proteins - biosynthesis
Fungal Proteins - genetics
GENE
GENE EXPRESSION
GENES
Genetic Complementation Test
INITIATION
Molecular Sequence Data
MUTACION
MUTATION
Proline - physiology
Protein Kinases - biosynthesis
Protein Kinases - genetics
PROTEIN SYNTHESIS
PROTEINAS
PROTEINE
PROTEINS
SACCHAROMYCES CEREVISIAE
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae Proteins
Schizosaccharomyces - genetics
SCHIZOSACCHAROMYCES POMBE
Sequence Homology, Amino Acid
YEAST
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Description
Summary:The gamma subunit of eukaryotic translation initiation factor 2 is an EF-Tu-like protein that plays an essential role in protein synthesis. We have isolated an eIF-2gamma homolog from the fission yeast Schizosaccharomyces pombe that complements a gcd11 null allele in Saccharomyces cerevisiae. GCD11 is an essential gene that encodes S. cerevisiae eIF-2gamma. Comparison among three eIF-2gamma homologs from humans, S. cerevisiae, and S. pombe, and a putative Drosophila homolog, reveals the presence of a domain N-terminal to the GTP-binding (G) domain that varies in length (relative to EF-Tu) from 12 residues in S. pombe to 89 residues in S. cerevisiae. In S. cerevisiae, these sequences are not essential for function. However, unlike a deletion, a missense mutation in this domain confers a slow growth phenotype and constitutively derepresses expression of the GCN4 transcriptional activator. The eIF-2gamma homologs also contain a partially conserved 35-37 amino acid insertion in the G domain that is absent from EF-Tu and other G proteins. Unlike the variable N-terminal domain, these residues are required for the essential function of eIF-2gamma.
ISSN:0026-8925
1432-1874