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Structure and Mechanism of the trp Repressor/Operator System

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Nucleic Acids and Molecular Biology

Part of the book series: Nucleic Acids and Molecular Biology ((NUCLEIC,volume 3))

Abstract

The trp aporepressor of Escherichia coli exists as a homodimer of two 107-amino acid chains and is activated to the trp repressor by the non-cooperative binding of two molecules of the co-repressor, L-tryptophan (Joachimiak et al. 1983). Once activated, the trp repressor binds with specificity and high affinity (Joachimiak et al. 1983; Klig et al. 1987; Carey 1988) to the operators of three operons, preventing initiation of transcription. These operons are: trpEDCBA, which encodes the enzymes committed to L-tryptophan biosynthesis; aroH,which encodes one of the isozymes for the first step in aromatic amino acid biosynthesis; and trpR, which encodes the trp aporepressor protein (Joachimiak et al. 1983; Somerville 1983).

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Author notes

  1. P. B. Sigler

    Present address: Department of Molecular Biophysics and Biochemistry, and the Howard Hughes Medical Institute, Yale University, 260 Whitney Avenue, New Haven, Connecticut, 06511, USA

Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology and Department of Chemistry, The University of Chicago, Chicago, Illinois, 60637, USA

    P. B. Sigler

Authors
  1. R. Q. Marmorstein
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  2. P. B. Sigler
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Editors and Affiliations

  1. Abteilung Chemie, Max-Planck-Institut für experimentelle Medizin, Hermann-Rein-Straße 3, 3400, Göttingen, Germany

    Fritz Eckstein

  2. Biochemistry Department, University of Dundee, DD1 4HN, Dundee, UK

    David M. J. Lilley

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© 1989 Springer-Verlag Berlin Heidelberg

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Marmorstein, R.Q., Sigler, P.B. (1989). Structure and Mechanism of the trp Repressor/Operator System. In: Eckstein, F., Lilley, D.M.J. (eds) Nucleic Acids and Molecular Biology. Nucleic Acids and Molecular Biology, vol 3. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-83709-8_5

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  • DOI: https://doi.org/10.1007/978-3-642-83709-8_5

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-83711-1

  • Online ISBN: 978-3-642-83709-8

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