Evidence map›Paper›PMID 21764926›Full record

ArticleJournal of bacteriology2011

The 5.5 protein of phage T7 inhibits H-NS through interactions with the central oligomerization domain.

Sabrina S Ali, Emily Beckett, Sandy Jeehoon Bae, William Wiley Navarre

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.0field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Review
  3. AInternational journal of molecular sciences · 2023
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  12. Transcription of Bacterial Chromatin.Journal of molecular biology · 2019
    Review
  13. Article
  14. TheViruses · 2018
    Article
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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.

Sabrina S AliDepartment of Molecular Genetics, University of Toronto, Toronto, Ontario, M5S 1A8 Canada.
Emily Beckett
Sandy Jeehoon Bae
William Wiley Navarre
University of Toronto · CA

Funding

Canadian Institutes of Health Research MOP-86683Canadian Institutes of Health Research MSH-87729
6 · The paper itself

Abstract

The 5.5 protein (T7p32) of coliphage T7 (5.5(T7)) was shown to bind and inhibit gene silencing by the nucleoid-associated protein H-NS, but the mechanism by which it acts was not understood. The 5.5(T7) protein is insoluble when expressed in Escherichia coli, but we find that 5.5(T7) can be isolated in a soluble form when coexpressed with a truncated version of H-NS followed by subsequent disruption of the complex during anion-exchange chromatography. Association studies reveal that 5.5(T7) binds a region of H-NS (residues 60 to 80) recently found to contain a distinct domain necessary for higher-order H-NS oligomerization. Accordingly, we find that purified 5.5(T7) can disrupt higher-order H-NS-DNA complexes in vitro but does not abolish DNA binding by H-NS per se. Homologues of the 5.5(T7) protein are found exclusively among members of the Autographivirinae that infect enteric bacteria, and despite fairly low sequence conservation, the H-NS binding properties of these proteins are largely conserved. Unexpectedly, we find that the 5.5(T7) protein copurifies with heterogeneous low-molecular-weight RNA, likely tRNA, through several chromatography steps and that this interaction does not require the DNA binding domain of H-NS. The 5.5 proteins utilize a previously undescribed mechanism of H-NS antagonism that further highlights the critical importance that higher-order oligomerization plays in H-NS-mediated gene repression.

Indexed as

Protein Interaction MappingBacteriophage T7Escherichia coliEscherichia coli ProteinsFimbriae ProteinsProtein BindingProtein Structure, TertiaryViral ProteinsEscherichia coli ProteinsFimbriae ProteinsFimG protein, E coligene 5.5 protein, Bacteriophage T7Viral Proteins

Identifiers

PMID21764926
PMCPMC3165711
OpenAlexW2129254575

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.