Modification of 40S ribosomal subunits from yeast with dimethylmaleic anhydride.
Modification of 40S ribosomal subunits from Saccharomyces cerevisiae with dimethylmaleic anhydride (DMMA), a reagent for protein amino groups, is accompanied by loss of polypeptide-synthesizing activity and by dissociation of proteins from the particles. The protein-deficient ribosomal particles, originated from 40S subunits by treatment with dimethylmaleic anhydride at a molar ratio of reagent to particle of 250, can partially reconstitute active subunits upon addition of the corresponding released proteins, and regeneration of the modified amino groups.
D000643:Ammonium Chloride / Q000494:pharmacology; D005663:Furans / Q000494:pharmacology*; D007700:Kinetics; D008299:Maleic Anhydrides / Q000494:pharmacology*; D010452:Peptide Biosynthesis; D010455:Peptides; D012269:Ribosomal Proteins / Q000032:analysis; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000378:metabolism*
D005663:Furans; D008299:Maleic Anhydrides; D010455:Peptides; D012269:Ribosomal Proteins; D000643:Ammonium Chloride; C012001:polyphenylalanine; C007474:2,3-dimethylmaleic anhydride