Evidence map›Paper›PMID 22934834›Full record

ArticleMolecular microbiology2012

Inhibitory mechanism of the Qβ lysis protein A2.

C A Reed, C Langlais, V Kuznetsov, R Young

Abstract read
In one paragraph

Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

17 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Engineered Proteins Mimic ssRNA Phage to Disrupt Type IV Pili.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Physiological characterization of single gene lysis proteins.bioRxiv : the preprint server for biology · 2023
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Single-gene lysis in the metagenomic era.Current opinion in microbiology · 2020
    Review
  12. Review
  13. Review
  14. Article
  15. Asymmetric cryo-EM structure of the canonical Allolevivirus Qβ reveals a single maturation protein and the genomic ssRNA in situ.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  16. Review
  17. 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.

C A ReedDepartment of Biochemistry and Biophysics, Texas A&M University, 2128 TAMU, College Station, TX 77843-2128, USA.
C Langlais
V Kuznetsov
R Young
Texas A&M University · US

Funding

CONTROL OF VIRUS-INDUCED LYSISR01GM027099 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI YOUNG, RYLAND FLETCHER · 1985 to 2019
$4.6M
CONTROL OF VIRUS INDUCED LYSISR37GM027099 · NIGMS · TEXAS A&M UNIVERSITY SYSTEM · PI YOUNG, RYLAND F. · 1996 to 2005
$2.4M
NIGMS NIH HHS GM27099NIGMS NIH HHS R01 GM027099NIGMS NIH HHS R37 GM027099
6 · The paper itself

Abstract

The lysis protein A2 , present as a single copy on the surface of Qβ virion particles, was previously shown to inhibit the activity of MurA, an enzyme that catalyses the first committed step of murein biosynthesis. Here we report experiments with a two-hybrid study that indicates A2 and MurA interact directly. Moreover, experiments with a soluble MBP-A2 fusion indicate that the interaction between MurA and A2 is dependent on a substrate-induced conformational change featured in the UDP-NAG-liganded state of MurA but not the tetrahedral intermediate state. Moreover, based on the location of L138Q, the original dominant A2 -resistant mutant that identified MurA as the target, a directed mutagenesis strategy has identified a continuous surface required for A2 binding. This surface spans the catalytic loop/cleft and encompasses both the catalytic and C-terminal domains. These data support a model in which A2 preferentially binds MurA liganded with UDP-NAG, thereby preventing catalysis by occluding PEP from accessing the active site.

Indexed as

Alkyl and Aryl TransferasesAllolevivirusDNA Mutational AnalysisEnzyme InhibitorsEscherichia coliModels, MolecularProtein BindingProtein ConformationTwo-Hybrid System TechniquesViral ProteinsAlkyl and Aryl TransferasesEnzyme InhibitorsUDP-N-acetylglucosamine 1-carboxyvinyltransferaseViral Proteins

Identifiers

PMID22934834
PMCPMC4631118
OpenAlexW1851437912

What OpenQuestion holds

Textmetadata
LicenceTDM
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.