A Specific Inhibitor of Polypeptide-Chain Initiation in Escherichia coli

  1. Sylvia Lee-Huang,
  2. Henry Lee, and
  3. Severo Ochoa*
  1. 1Department of Biochemistry, New York University School of Medicine, New York, N.Y. 10016

Abstract

An inhibitor of polypeptide-chain initiation was isolated from E. coli cells. This protein inhibits formation of the 30S or 70S initiation complex with either fMet-tRNAf as initiator and AUG, MS2 RNA, or late T4 RNA as messenger, or acPhe-tRNA as initiator and poly(U) as messenger. Chain elongation, e.g., poly(U) translation at high Mg2+ concentration, is not inhibited. The inhibitor is rendered ineffective when active aminoacylation of tRNA is taking place, e.g., during natural mRNA translation. This inhibitor is distinct from the so-called interference (i) factors, which interfere exclusively with the action of initiation factor 3. Since the new inhibitor can apparently be turned on and off, it may have a regulatory function in translation.

Footnotes

  • * To whom reprint requests should be sent.

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