Insulin promoted decrease in the phosphorylation of protein synthesis initiation factor eIF-2

1984 ◽  
Vol 121 (1) ◽  
pp. 134-140 ◽  
Author(s):  
C.A. Towle ◽  
H.J. Mankin ◽  
J. Avruch ◽  
B.V. Treadwell
1989 ◽  
Vol 264 (31) ◽  
pp. 18527-18530 ◽  
Author(s):  
Z Smit-McBride ◽  
J Schnier ◽  
R J Kaufman ◽  
J W Hershey

1987 ◽  
Vol 7 (3) ◽  
pp. 998-1003
Author(s):  
M Altmann ◽  
C Handschin ◽  
H Trachsel

We have isolated genomic and cDNA clones encoding protein synthesis initiation factor eIF-4E (mRNA cap-binding protein) of the yeast Saccharomyces cerevisiae. Their identity was established by expression of a cDNA in Escherichia coli. This cDNA encodes a protein indistinguishable from purified eIF-4E in terms of molecular weight, binding to and elution from m7GDP-agarose affinity columns, and proteolytic peptide pattern. The eIF-4E gene was isolated by hybridization of cDNA to clones of a yeast genomic library. The gene lacks introns, is present in one copy per haploid genome, and encodes a protein of 213 amino acid residues. Gene disruption experiments showed that the gene is essential for growth.


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