Abstract
The function of ribosomal protein S21 in protein synthesis has been examined by (a) inactivation of S21 in situ with specific antibodies and (b) the use of 30-S subunits reconstituted in the absence of S21. The results from the two approaches are consistent, 30-S subunits treated with anti-S21 or lacking S21 are still active in the translation of poly(U) or poly(A, G, U). They are also functional in fMet-tRNA binding when directed by poly(A, G, U) or the AUG triplet. They are not active in the translation of MS2 RNA or Escherichia coli mRNA. The defect of S21-deficient 30-S ribosomes can be traced back to their inability to bind MS2 RNA at the initiation step of protein synthesis. Addition of S21 to S21-deprived subunits restores the MS2-RNA-dependent initiation complex formation.
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