Journal of Molecular Biology
Volume 186, Issue 4, 20 December 1985, Pages 707-713
Journal home page for Journal of Molecular Biology

Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli: I. Primary structure of a pyrI gene encoding a modified regulatory subunit

https://doi.org/10.1016/0022-2836(85)90390-0Get rights and content

Abstract

In a previous article, we have identified a lambda bacteriophage directing the synthesis of a modified aspartate carbamoyltransferase lacking substrate-co-operative interactions and insensitive to the feedback inhibitor CTP. These abnormal properties were ascribed to a mutation in the gene pyrI encoding the regulatory polypeptide chain of the enzyme. We now report the sequence of the mutated pyrI and show that, during the generation of this pyrBI-bearing phage, six codons from lambda DNA have been substituted for the eight terminal codons of the wild-type gene. A model is presented for the formation of this modified pyrI gene during the integrative recombination of the parental lambda phage with the Escherichia coli chromosome. An accompanying paper emphasizes the importance of the carboxy-terminal end of the regulatory chain for the homotropic and heterotropic interactions of aspartate carbamoyltransferase.

References (73)

  • M. Crabeel et al.

    Gene

    (1979)
  • C.A. Enns et al.

    J. Biol. Chem

    (1978)
  • C.A. Enns et al.

    J. Biol. Chem

    (1979)
  • J.C. Gerhart
  • J.C. Gerhart et al.

    J. Biol. Chem

    (1962)
  • D. Gigot et al.

    FEBS Letters

    (1977)
  • J.H. Griffin et al.

    J. Biol. Chem

    (1973)
  • G. Hervé et al.

    J. Mol. Biol

    (1985)
  • R.B. Honzatko et al.

    J. Mol. Biol

    (1982)
  • R.B. Honzatko et al.

    J. Mol. Biol

    (1982)
  • G.R. Jacobson et al.
  • E.R. Kantrowitz et al.

    J. Biol. Chem

    (1977)
  • E.R. Kantrowitz et al.

    Trends Biochem. Sci

    (1980)
  • E.R. Kantrowitz et al.

    Trends Biochem. Sci

    (1980)
  • E.R. Kantrowitz et al.

    J. Mol. Biol

    (1981)
  • D. Kerbiriou et al.

    J. Mol. Biol

    (1972)
  • D. Kerbiriou et al.

    J. Mol. Biol

    (1973)
  • D. Kerbiriou et al.

    J. Biol. Chem

    (1977)
  • M. Ladjimi et al.

    J. Mol. Biol

    (1985)
  • M. Mandel et al.

    J. Mol. Biol

    (1970)
  • A. Maxam et al.

    Methods Enzymol

    (1980)
  • D.K. McClintock et al.

    J. Biol. Chem

    (1968)
  • D.K. McClintock et al.

    J. Biol. Chem

    (1969)
  • J. Monod et al.

    J. Mol. Biol

    (1965)
  • B. Perbal et al.

    J. Mol. Biol

    (1972)
  • B. Perbal et al.

    J. Mol. Biol

    (1977)
  • W. Ross et al.

    Cell

    (1983)
  • W. Ross et al.

    Cell

    (1979)
  • R.S. Silver et al.

    J. Mol. Biol

    (1983)
  • P. Tauc et al.

    J. Mol. Biol

    (1982)
  • L. Thiry et al.

    J. Mol. Biol

    (1978)
  • R.A. Yates et al.

    J. Biol. Chem

    (1956)
  • J.P. Changeux et al.

    Biochemistry

    (1968)
  • J.P. Changeux et al.

    Biochemistry

    (1968)
  • J.A. Cohlberg et al.

    Biochemistry

    (1972)
  • R. Cunin et al.

    Arch. Intern. Physiol. Biochim

    (1984)
  • Cited by (12)

    View all citing articles on Scopus

    This work was supported by the Fonds de la Recherche Fondamentale Collective-Fonds voor Kollektief Fundamenteel Onderzoek (contract 2.9012.83) as well as by an “Action de Recherche Concertée-Onderling Overlegde Aktie” between the Free Universities of Brussels and the Belgian Government.

    View full text