Journal of Molecular Biology
Volume 90, Issue 4, 25 December 1974, Pages 727-732, IN37-IN40, 733-738
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Control by bacteriophage T4 of two sequential phosphorylations of the alpha subunit of Escherichia coli RNA polymerase

https://doi.org/10.1016/0022-2836(74)90536-1Get rights and content

Abstract

Coliphage T4 induces two distinct phosphorylations of the α subunit of the host RNA polymerase. The first, termed alteration, requires injection but not expression of the phage genome and may be catalyzed by an activity carried in the virion. Alteration of α proceeds in the absence of RNA or protein synthesis but is not induced by phage ghosts. Alteration occurs very early during the course of a normal T4 infection. Kinetically coincident with α alteration are phosphorylations of other subunits of RNA polymerase, including sigma. Occurring slightly later than alteration is a second T4-induced phosphorylation of α, termed modification. Modification requires phage-specific protein synthesis and probably involves a T4 “quasi-late” function. Virtually all α polypeptides are “modified” by seven minutes after infection at 30 °C and remain modified throughout the T4 life-cycle.

References (52)

  • M. Adesnik et al.

    J. Mol. Biol

    (1970)
  • G. Ames

    J. Biol. Chem

    (1974)
  • E. Bautz et al.

    Biochem. Biophys. Res. Commun

    (1969)
  • D. Berg et al.
  • A. Bolle et al.

    J. Mol. Biol

    (1968)
  • A. Bolle et al.

    J. Mol. Biol

    (1968)
  • H. Bremer et al.

    J. Mol. Biol

    (1973)
  • R. Burgess

    J. Biol. Chem

    (1969)
  • D. Dalbow

    J. Mol. Biol

    (1973)
  • D. Duckworth

    Virology

    (1970)
  • C. Goff

    J. Biol. Chem

    (1974)
  • A. Guha et al.

    J. Mol. Biol

    (1971)
  • A. Hirashima et al.

    J. Mol. Biol

    (1973)
  • R. Kaempfer et al.

    J. Mol. Biol

    (1967)
  • H. Matzura et al.

    J. Mol. Biol

    (1973)
  • S. Mizuno et al.

    Biochem. Biophys. Res. Commun

    (1969)
  • M. Nomura et al.

    J. Mol. Biol

    (1962)
  • G. Notani

    J. Mol. Biol

    (1973)
  • P. O'Farrell et al.

    J. Biol. Chem

    (1973)
  • P. O'Farrell et al.

    J. Biol. Chem

    (1973)
  • J. Pulitzer

    J. Mol. Biol

    (1970)
  • J. Pulitzer et al.

    J. Mol. Biol

    (1970)
  • W. Salser et al.

    J. Mol. Biol

    (1970)
  • W. Seifert et al.

    FEBS Letters

    (1971)
  • P. Strigini et al.

    J. Mol. Biol

    (1973)
  • G. Walter et al.

    Biochem. Biophys. Res. Commun

    (1968)
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    This research was supported by National Institutes of Health grant no. GM09541 to Dr W. Gilbert.

    Present address: Medical Research Council, Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, England.

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