Altered mRNA cap recognition activity of initiation factor 4E in the yeast cell cyde division mutant cdc33

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Abstract
The mutation in the S.cerevisiae cell cycle division mutant cdc33 consists of a single G to A transition in the open reading frame encoding translation initiation factor 4E (eIF-4E). This leads to the substitution of glycine113 by aspartic acid close to tryptophane 115 in the protein. This mutation reduces cap binding activity of eUM-4E as measured by binding of eIF-4E to m7GDP agarose columns and slows down overall protein synthesis at the non-permissive temperature. Comparison of the cdc33 mutation with other mutations affecting eIF-4E function supports the view that tryptophane residues and their flanking regions are involved in cap binding activity of eIF-4E.