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

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.

authors

Kim HC,Zhou JG,Wilson HR,Mogilnitskiy G,Court DL,Gottesman ME

doi

10.1073/pnas.0430995100

keywords:

subject

Has Abstract

pub_date

2003-04-29 00:00:00

pages

5308-12

issue

9

eissn

0027-8424

issn

1091-6490

pii

0430995100

journal_volume

100

pub_type

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