title: Structure and function of initiation complexes which accumulate during inhibition of protein synthesis by fluoride ion.
abstract: Incubation of the reticulocyte lysate cell-free system with KF results in the accumulation in polysomes of complexes containing deacylated tRNAMet and of complexes which can initiate globin chains in the presence of aurintricarboxylate. Degradation of these polysomes with T1RNase yields both 40 S and 80 S particles, and tRNAMet is found in both of these fractions. When the 80 S particles are reincubated with the soluble fraction of the lysate plus reagents for protein synthesis, short peptides which have the properties of the NH2-terminal regions of globin are synthesized de novo. These peptides are deficient in NH2-terminal methionine, but occur under conditions where nascent globin peptides of comparable length, containing NH2-terminal methionine, are completely protected from the methionine aminopeptidase.
mesh_terms: D000818:Animals; D001798:Blood Proteins / Q000096:biosynthesis; D003488:Cyanogen Bromide; D005459:Fluorides / Q000494:pharmacology*; D010446:Peptide Fragments / Q000032:analysis; D010448:Peptide Initiation Factors; D011132:Polyribosomes / Q000187:drug effects / Q000378:metabolism; D014176:Protein Biosynthesis / Q000187:drug effects*; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism
chemical_list: D001798:Blood Proteins; D010446:Peptide Fragments; D010448:Peptide Initiation Factors; D003488:Cyanogen Bromide; D005459:Fluorides