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Phage HK022 nun protein represses translation of phage lambda N (transcription termination/translation repression)

  1. Author:
    Kim, H. C.
    Zhou, J. G.
    Wilson, H. R.
    Mogilnitskiy, G.
    Court, D. L.
    Gottesman, M. E.

  2. Author Address

    Columbia Univ, Coll Phys & Surg, Dept Biochem & Mol Biophys, New York, NY 10032 USA Columbia Univ, Coll Phys & Surg, Dept Biochem & Mol Biophys, New York, NY 10032 USA Columbia Univ Coll Phys & Surg, Canc Res Inst, New York, NY 10032 USA NCI, Mol Control & Genet Sect, NIH, Frederick, MD 21702 USA Inst Biotechnol, Beijing 100850, Peoples R China Gottesman ME Columbia Univ, Coll Phys & Surg, Dept Biochem & Mol Biophys, New York, NY 10032 USA
    1. Year: 2003
  2. Journal: Proceedings of the National Academy of Sciences of the United States of America
    1. 100
    2. 9
    3. Pages: 5308-5312
  4. Type of Article: Article
  1. Abstract:

    The N-terminal arginine-rich motif of phage HK022 Nun protein binds to NUT sequences in phage A nascent transcripts and induces transcription termination. Interactions between the Nun C terminus and RNA polymerase as well as the DNA template are required for termination. We have isolated Nun C-terminal point and deletion mutants that are unable to block transcription. The mutants bind NUT RNA and inhibit translation of the lambda N gene. Thus HK022 excludes A both by terminating transcription on the phage chromosome and by preventing translation of the essential A N gene. Like N autoregulation, translation repression by Nun requires host RNaseIII deficiency (rnc) or a mutation in the RNaseIII processing site (rIII) located between NUTL and the beginning of the N coding sequence. Our data support the idea that Nun bound at NUTL causes steric interference with ribosome attachment to the nearby IN coding sequence. Two models, Nun acting alone or in complex with host proteins, are discussed.

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