The Nun protein of bacteriophage HK022 inhibits translocation of Escherichia coli RNA polymerase without abolishing its catalytic activities

Siu Chun Hung, Max E. Gottesman*

*Corresponding author for this work

Research output: Contribution to journalJournal Articlepeer-review

25 Citations (Scopus)

Abstract

Bacteriophage HK022 Nun protein blocks transcription elongation by Escherichia coli RNA polymerase in vitro without dissociating the transcription complex. Nun is active on complexes located at any template site tested. Ultimately, only the 3'-OH terminal nucleotide of the nascent transcript in an arrested complex can turn over; it is removed by pyrophosphate and restored with NTPs. This suggests that Nun inhibits the translocation of RNA polymerase without abolishing its catalytic activities. Unlike spontaneously arrested complexes, Nun-arrested complexes cannot be reactivated by transcription factor GreB. The various complexes show distinct patterns of nucleotide incorporation and pyrophosphorolysis before or after treatment with Nun, suggesting that the configuration of RNAP, transcript, and template DNA is different in each complex.

Original languageEnglish
Pages (from-to)2670-2678
Number of pages9
JournalGenes and Development
Volume11
Issue number20
DOIs
Publication statusPublished - 15 Oct 1997
Externally publishedYes

Keywords

  • Nun protein
  • Phage HK022
  • RNA polymerase
  • Transcription arrest
  • Translocation

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