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. 1970 Aug;66(4):1027–1035. doi: 10.1073/pnas.66.4.1027

SPECIFIC BINDING OF LEUCYL TRANSFER RNA TO AN IMMATURE FORM OF L-THREONINE DEAMINASE: ITS IMPLICATIONS IN REPRESSION*

G Wesley Hatfield 1,†, R O Burns 1,‡
PMCID: PMC335782  PMID: 4920088

Abstract

The in vitro assembly of L-threonine deaminase from its constituent parts results in the formation of an inactive species of this enzyme which specifically and reversibly binds leucyl-tRNA. The native, catalytically active enzyme, which is derived from this species in the presence of maturation-inducing ligands, does not bind tRNA. The possible involvement of this protein-tRNA complex in the repression of the ilv (ADE) operon is discussed.

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Selected References

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

  1. Arfin S. M., Ratzkin B., Umbarger H. E. The metabolism of valine and isoleucine in Escherichia coli. XVII. The role of induction in the derepression of acetohydroxy acid isomeroreductase. Biochem Biophys Res Commun. 1969 Dec 4;37(6):902–908. doi: 10.1016/0006-291x(69)90216-2. [DOI] [PubMed] [Google Scholar]
  2. Burns R. O., Zarlengo M. H. Threonine deaminase from Salmonella typhimurium. I. Purification and properties. J Biol Chem. 1968 Jan 10;243(1):178–185. [PubMed] [Google Scholar]
  3. EIDLIC L., NEIDHARDT F. C. ROLE OF VALYL-SRNA SYNTHETASE IN ENZYME REPRESSION. Proc Natl Acad Sci U S A. 1965 Mar;53:539–543. doi: 10.1073/pnas.53.3.539. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Gilbert W., Müller-Hill B. Isolation of the lac repressor. Proc Natl Acad Sci U S A. 1966 Dec;56(6):1891–1898. doi: 10.1073/pnas.56.6.1891. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hatfield G. W., Burns R. O. Threonine deaminase from Salmonella typhimurium. 3. The intermediate substructure. J Biol Chem. 1970 Feb 25;245(4):787–791. [PubMed] [Google Scholar]
  6. Ito K., Hiraga S., Yura T. Tryptophanyl transfer RNA synthetase and expression of the tryptophan operon in the trpS mutants of Escherichia coli. Genetics. 1969 Mar;61(3):521–538. doi: 10.1093/genetics/61.3.521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Kovach J. S., Phang J. M., Ference M., Goldberger R. F. Studies on repression of the histidine operon. II. The role of the first enzyme in control of the histidine system. Proc Natl Acad Sci U S A. 1969 Jun;63(2):481–488. doi: 10.1073/pnas.63.2.481. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. LITTAUER U. Z., KORNBERG A. Reversible synthesis of polyribonucleotides with an enzyme from Escherichia coli. J Biol Chem. 1957 Jun;226(2):1077–1092. [PubMed] [Google Scholar]
  9. Maeba P., Sanwal B. D. The allosteric threonine deaminase of Salmonella. Kinetic model for the native enzyme. Biochemistry. 1966 Feb;5(2):525–536. doi: 10.1021/bi00866a019. [DOI] [PubMed] [Google Scholar]
  10. Roth J. R., Ames B. N. Histidine regulatory mutants in Salmonella typhimurium II. Histidine regulatory mutants having altered histidyl-tRNA synthetase. J Mol Biol. 1966 Dec 28;22(2):325–333. doi: 10.1016/0022-2836(66)90135-5. [DOI] [PubMed] [Google Scholar]
  11. SOMERVILLE R. L., YANOFSKY C. STUDIES ON THE REGULATION OF TRYPTOPHAN BIOSYNTHESIS IN ESCHERICHIA COLI. J Mol Biol. 1965 Apr;11:747–759. doi: 10.1016/s0022-2836(65)80032-8. [DOI] [PubMed] [Google Scholar]
  12. Szentirmai A., Szentirmai M., Umbarger H. E. Isoleucine and valine metabolism of Escherichia coli. XV. Biochemical properties of mutants resistant to thiaisoleucine. J Bacteriol. 1968 May;95(5):1672–1679. doi: 10.1128/jb.95.5.1672-1679.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Zarlengo M. H., Robinson G. W., Burns R. O. Threonine deaminase from Salmonella typhimurium. II. The subunit structure. J Biol Chem. 1968 Jan 10;243(1):186–191. [PubMed] [Google Scholar]

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