Abstract:
:The N-terminal arginine-rich motif of phage HK022 Nun protein binds to NUT sequences in phage lambda 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 lambda both by terminating transcription on the phage chromosome and by preventing translation of the essential lambda 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 N coding sequence. Two models, Nun acting alone or in complex with host proteins, are discussed.
journal_name
Proc Natl Acad Sci U S Aauthors
Kim HC,Zhou JG,Wilson HR,Mogilnitskiy G,Court DL,Gottesman MEdoi
10.1073/pnas.0430995100keywords:
subject
Has Abstractpub_date
2003-04-29 00:00:00pages
5308-12issue
9eissn
0027-8424issn
1091-6490pii
0430995100journal_volume
100pub_type
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