Characterization of a 40S ribosomal subunit complex in polyribosomes of Saccharomyces cerevisiae treated with cycloheximide.
Under specific conditions cycloheximide treatment of Saccharomyces cerevisiae caused the accumulation of a type of polyribosome called "halfmer." Limited ribonuclease digestion of halfmers released particles from the polyribosomes identified as 40S ribosomal subunits. The data demonstrated that halfmers are polyribosomes containing an additional 40S ribosomal subunit attached to the messenger ribonucleic acid. Protein gel electrophoretic analysis of halfmers revealed numerous nonribosomal proteins. Two of these proteins comigrate with subunits of yeast initiation factor eIF2.
D003513:Cycloheximide / Q000494:pharmacology*; D015852:Eukaryotic Initiation Factor-2; D005656:Fungal Proteins / Q000302:isolation & purification; D008968:Molecular Conformation; D010448:Peptide Initiation Factors / Q000302:isolation & purification; D011132:Polyribosomes / Q000187:drug effects* / Q000378:metabolism; D011506:Proteins / Q000302:isolation & purification; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000187:drug effects* / Q000378:metabolism
D015852:Eukaryotic Initiation Factor-2; D005656:Fungal Proteins; D010448:Peptide Initiation Factors; D011506:Proteins; D003513:Cycloheximide