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. 1973 Oct;70(10):2874–2878. doi: 10.1073/pnas.70.10.2874

A Specific Inhibitor of Polypeptide-Chain Initiation in Escherichia coli

Sylvia Lee-Huang 1, Henry Lee 1, Severo Ochoa 1,*
PMCID: PMC427129  PMID: 4583026

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.

Keywords: initiation factors, regulation, translation regulation

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Cuzin F., Kretchmer N., Greenberg R. E., Hurwitz R., Chapeville F. Enzymatic hydrolysis of N-substituted aminoacyl-tRNA. Proc Natl Acad Sci U S A. 1967 Nov;58(5):2079–2086. doi: 10.1073/pnas.58.5.2079. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Groner Y., Pollack Y., Berissi H., Revel M. Cistron specific translation control protein in Escherichia coli. Nat New Biol. 1972 Sep 6;239(88):16–19. doi: 10.1038/newbio239016a0. [DOI] [PubMed] [Google Scholar]
  3. Groner Y., Scheps R., Kamen R., Kolakofsky D., Revel M. Host subunit of Q replicase is translation control factor i. Nat New Biol. 1972 Sep 6;239(88):19–20. doi: 10.1038/newbio239019a0. [DOI] [PubMed] [Google Scholar]
  4. Haseltine W. A., Block R., Gilbert W., Weber K. MSI and MSII made on ribosome in idling step of protein synthesis. Nature. 1972 Aug 18;238(5364):381–384. doi: 10.1038/238381a0. [DOI] [PubMed] [Google Scholar]
  5. Haseltine W. A., Block R. Synthesis of guanosine tetra- and pentaphosphate requires the presence of a codon-specific, uncharged transfer ribonucleic acid in the acceptor site of ribosomes. Proc Natl Acad Sci U S A. 1973 May;70(5):1564–1568. doi: 10.1073/pnas.70.5.1564. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kamen R. Characterization of the subunits of Q-beta replicase. Nature. 1970 Nov 7;228(5271):527–533. doi: 10.1038/228527a0. [DOI] [PubMed] [Google Scholar]
  7. Kamen R., Kondo M., Römer W., Weissmann C. Reconstitution of Q replicase lacking subunit with protein-synthesis-interference factor i. Eur J Biochem. 1972 Nov 21;31(1):44–51. doi: 10.1111/j.1432-1033.1972.tb02498.x. [DOI] [PubMed] [Google Scholar]
  8. Kondo M., Gallerani R., Weissmann C. Subunit structure of Q-beta replicase. Nature. 1970 Nov 7;228(5271):525–527. doi: 10.1038/228525a0. [DOI] [PubMed] [Google Scholar]
  9. Lee-Huang S., Ochoa S. Messenger discriminating species of initiation factor F3. Nat New Biol. 1971 Dec 22;234(51):236–239. doi: 10.1038/newbio234236a0. [DOI] [PubMed] [Google Scholar]
  10. Lee-Huang S., Ochoa S. Purification and properties of two messenger-discriminating species of E. coli initiation factor 3. Arch Biochem Biophys. 1973 May;156(1):84–96. doi: 10.1016/0003-9861(73)90344-5. [DOI] [PubMed] [Google Scholar]
  11. Lee-Huang S., Ochoa S. Specific inhibitors of MS2 and late T4 RNA translation in E. coli. Biochem Biophys Res Commun. 1972 Oct 17;49(2):371–376. doi: 10.1016/0006-291x(72)90420-2. [DOI] [PubMed] [Google Scholar]
  12. Lee-Huang S., Sillero M. A., Ochoa S. Isolation and properties of crystalline initiation factor F1 from Escherichia coli ribosomes. Eur J Biochem. 1971 Feb;18(4):536–543. doi: 10.1111/j.1432-1033.1971.tb01274.x. [DOI] [PubMed] [Google Scholar]
  13. Legault L., Jeantet C., Gros F. Inhibition of in vitro protein synthesis by ppGpp. FEBS Lett. 1972 Oct 15;27(1):71–75. doi: 10.1016/0014-5793(72)80412-5. [DOI] [PubMed] [Google Scholar]
  14. Lucas-Lenard J., Lipmann F. Initiation of polyphenylalanine synthesis by N-acetylphenylalanyl-SRNA. Proc Natl Acad Sci U S A. 1967 Apr;57(4):1050–1057. doi: 10.1073/pnas.57.4.1050. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Manzocchi L. A., Tarragó A., Allende J. E. The effect of ppGpp on in vitro protein synthesis by a wheat embryo system. FEBS Lett. 1973 Feb 1;29(3):309–312. doi: 10.1016/0014-5793(73)80046-8. [DOI] [PubMed] [Google Scholar]
  16. NIRENBERG M., LEDER P. RNA CODEWORDS AND PROTEIN SYNTHESIS. THE EFFECT OF TRINUCLEOTIDES UPON THE BINDING OF SRNA TO RIBOSOMES. Science. 1964 Sep 25;145(3639):1399–1407. doi: 10.1126/science.145.3639.1399. [DOI] [PubMed] [Google Scholar]
  17. Pedersen F. S., Lund E., Kjeldgaard N. O. Codon specific, tRNA dependent in vitro synthesis of ppGpp and pppGpp. Nat New Biol. 1973 May 2;243(122):13–15. [PubMed] [Google Scholar]
  18. Vaughan M. H., Jr, Pawlowski P. J., Forchhammer J. Regulation of protein synthesis initiation in HeLa cells deprived of single essential amino acids. Proc Natl Acad Sci U S A. 1971 Sep;68(9):2057–2061. doi: 10.1073/pnas.68.9.2057. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Vogel Z., Zamir A., Elson D. On the specificity and stability of an enzyme that hydrolyzes N-substituted aminoacyl-transfer RNA's. Proc Natl Acad Sci U S A. 1968 Oct;61(2):701–707. doi: 10.1073/pnas.61.2.701. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Yoshida M., Travers A., Clark B. F. Inhibition of translation initiation complex formation by MS1. FEBS Lett. 1972 Jun 15;23(2):163–166. doi: 10.1016/0014-5793(72)80331-4. [DOI] [PubMed] [Google Scholar]

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