Characterization of a 40S ribosomal subunit complex in polyribosomes of Saccharomyces cerevisiae treated with cycloheximide. | Zendy

Terry L. Helser | Zendy; Robert A. Baan | Zendy; Albert E. Dahĺberg | Zendy

Open Access

Characterization of a 40S ribosomal subunit complex in polyribosomes of Saccharomyces cerevisiae treated with cycloheximide.

Author(s) -

Terry L. Helser,

Robert A. Baan,

Albert E. Dahĺberg

Publication year - 1981

Publication title -

molecular and cellular biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.14

H-Index - 327

eISSN - 1067-8824

pISSN - 0270-7306

DOI - 10.1128/mcb.1.1.51

Subject(s) - eukaryotic large ribosomal subunit , biology , eukaryotic small ribosomal subunit , polysome , cycloheximide , ribosomal protein , ribosomal rna , saccharomyces cerevisiae , ribonuclease , eukaryotic ribosome , biochemistry , protein subunit , ribosome , 18s ribosomal rna , microbiology and biotechnology , protein biosynthesis , yeast , rna , gene

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.

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