Evidence map›Paper›PMID 18922547›Full record

ArticleJournal of molecular biology2008

The antitermination activity of bacteriophage lambda N protein is controlled by the kinetics of an RNA-looping-facilitated interaction with the transcription complex.

Clarke R Conant, Jim P Goodarzi, Steven E Weitzel, Peter H von Hippel

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.3field-weighted citation impact, top 34% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Engineered transcription-associated Cas9 targeting in eukaryotic cells.bioRxiv : the preprint server for biology · 2024
    Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Clarke R ConantInstitute of Molecular Biology and Department of Chemistry, University of Oregon, Eugene, OR 97403, USA.
Jim P Goodarzi
Steven E Weitzel
Peter H von Hippel
University of Oregon · US

Funding

STRUCTURE AND RELATIONS OF PROTEINS AND NUCLEIC ACIDSR01GM015792 · NIGMS · UNIVERSITY OF OREGON · PI MARCUS, ANDREW HADLEY · 1985 to 2025
$10.2M
MOLECULAR BIOLOGY AND BIOPHYSICST32GM007759 · NIGMS · UNIVERSITY OF OREGON · PI NOLEN, BRADLEY J · 1985 to 2021
$8.5M
MOLECULAR INTERACTION IN T4 DNA REPLICATION COMPLEXR01GM029158 · NIGMS · UNIVERSITY OF OREGON · PI VON HIPPEL, PETER HANS · 1985 to 2003
$1.2M
NIGMS NIH HHS R01 GM015792NIGMS NIH HHS R01 GM029158NIGMS NIH HHS T32 GM007759
6 · The paper itself

Abstract

Protein N of bacteriophage lambda activates the lytic phase of phage development in infected Escherichia coli cells by suppressing the activity of transcriptional terminators that prevent the synthesis of essential phage proteins. N binds tightly to the boxB RNA hairpin located near the 5' end of the nascent pL and pR transcripts and induces an antitermination response in the RNA polymerase (RNAP) of elongation complexes located at terminators far downstream. Here we test an RNA looping model for this N-dependent "action at a distance" by cleaving the nascent transcript between boxB and RNAP during transcript elongation. Cleavage decreases antitermination, showing that an intact RNA transcript is required to stabilize the interaction of boxB-bound N with RNAP during transcription. In contrast, an antitermination complex that also contains Nus factors retains N-dependent activity after transcript cleavage, suggesting that these host factors further stabilize the N-RNAP interaction. Thus, the binding of N alone to RNAP is controlled by an RNA looping equilibrium, but after formation of the initial RNA loop and in the presence of Nus factors the system no longer equilibrates on the transcription time scale, meaning that the "range" of antitermination activity along the template in the full antitermination system is kinetically controlled by the dissociation rate of the stabilized N-RNAP complex. Theoretical calculations of nucleic acid end-to-end contact probabilities are used to estimate the local concentrations of boxB-bound N at elongation complexes poised at terminators, and are combined with N activity measurements at various boxB-to-terminator distances to obtain an intrinsic affinity (K(d)) of approximately 2 x 10(-5) M for the N-RNAP interaction. This RNA looping approach is extended to include the effects of N binding at nonspecific RNA sites on the transcript and the implications for transcription control in other regulatory systems are discussed.

Indexed as

Nucleic Acid ConformationTranscription, GeneticBacteriophage lambdaBinding SitesCodon, TerminatorDNA-Directed RNA PolymerasesDNA, ViralKineticsModels, GeneticPeptide Elongation FactorsProtein BindingRNA, MessengerRNA, ViralTemplates, GeneticViral Regulatory and Accessory ProteinsCodon, TerminatorDNA-Directed RNA PolymerasesDNA, ViralN protein, Bacteriophage lambdaPeptide Elongation FactorsRNA, MessengerRNA, ViralViral Regulatory and Accessory Proteins

Identifiers

PMID18922547
PMCPMC2590625
OpenAlexW1970951396

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.