Altered mRNA cap recognition activity of initiation factor 4E in the yeast cell cycle division mutant cdc33.
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 glycine 113 by aspartic acid close to tryptophane 115 in the protein. This mutation reduces cap binding activity of eIF-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.
Altmann
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M
Institut für Biochemie und Molekularbiologie Universität Bern, Switzerland.
Trachsel
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H
D000595:Amino Acid Sequence; D001483:Base Sequence; D015153:Blotting, Western; D002455:Cell Division; D003001:Cloning, Molecular; D039561:Eukaryotic Initiation Factor-4E; D008969:Molecular Sequence Data; D009154:Mutation; D010448:Peptide Initiation Factors / Q000235:genetics / Q000378:metabolism*; D014176:Protein Biosynthesis; D012315:RNA Caps / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000235:genetics*; D013329:Structure-Activity Relationship; D014364:Tryptophan
D039561:Eukaryotic Initiation Factor-4E; D010448:Peptide Initiation Factors; D012315:RNA Caps; D012333:RNA, Messenger; D014364:Tryptophan