The Nun protein of bacteriophage HK022 inhibits translocation of Escherichia coliRNA polymerase without abolishing its catalytic activities
Open Access
- 15 October 1997
- journal article
- Published by Cold Spring Harbor Laboratory in Genes & Development
- Vol. 11 (20) , 2670-2678
- https://doi.org/10.1101/gad.11.20.2670
Abstract
Bacteriophage HK022 Nun protein blocks transcription elongation byEscherichia 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.Keywords
This publication has 28 references indexed in Scilit:
- Multiple interactions stabilize a single paused transcription intermediate in which hairpin to 3′ end spacing distinguishes pause and termination pathwaysJournal of Molecular Biology, 1997
- Three-dimensional structure of E. coil core RNA polymerase: Promoter binding and elongation conformations of the enzymeCell, 1995
- Phage HK022 Nun Protein Arrests Transcription on Phage λ DNA and Competes with the Phage λ N Antitermination ProteinJournal of Molecular Biology, 1995
- Discontinuous Mechanism of Transcription ElongationScience, 1994
- Transcript cleavage factors from E. coliCell, 1993
- Escherichia coli mutations that block transcription termination by phage HK022 Nun proteinJournal of Molecular Biology, 1991
- RNA chain elongation by Escherichia coli RNA polymeraseJournal of Molecular Biology, 1990
- λ nutR mutations convert HK022 nun protein from a transcription termination factor to a suppressor of terminationJournal of Molecular Biology, 1990
- The remarkable specificity of a new transcription termination factor suggests that the mechanisms of termination and antitermination are similarCell, 1987
- Procedure for the rapid, large-scale purification of Escherichia coli DNA-dependent RNA polymerase involving polymin P precipitation and DNA-cellulose chromatographyBiochemistry, 1975