Evidence map›Paper›PMID 21097630›Full record

ArticleJournal of bacteriology2011

Membrane topology and DNA-binding ability of the Streptococcal CpsA protein.

Brett R Hanson, Beth A Lowe, Melody N Neely

Open access · greenAbstract 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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 36 citations in OpenAlex.

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  7. Frontiers in microbiology · 2018
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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

3 authors at 1 institution in 1 country.

Brett R HansonDepartment of Immunology and Microbiology, Wayne State University School of Medicine, Detroit, MI 48201, USA.
Beth A Lowe
Melody N Neely
Wayne State University · US

Funding

Regulation of Virulence Gene Expression in ChlamydiaR01AI079083 · NIAID · UNIVERSITY OF KANSAS LAWRENCE · PI HEFTY, P SCOTT · 2010 to 2014
$1.8M
Streptococcal-Zebrafish Model of Bacterial PathogenesisR01AI052141 · NIAID · WAYNE STATE UNIVERSITY · PI NEELY, MELODY NEUHART · 2003 to 2006
$919k
Streptococcal-Zebrafish Model of Bacterial PathogenesisR21AI052141 · NIAID · WAYNE STATE UNIVERSITY · PI NEELY, MELODY NEUHART · 2002 to 2002
$259k
NIAID NIH HHS AI079083NIAID NIH HHS R01 AI052141NIAID NIH HHS R21 AI052141
6 · The paper itself

Abstract

Many streptococcal pathogens require a polysaccharide capsule for survival in the host during systemic infection. The highly conserved CpsA protein is proposed to be a transcriptional regulator of capsule production in streptococci, although the regulatory mechanism is unknown. Hydropathy plots of CpsA predict an integral membrane protein with 3 transmembrane domains and only 27 cytoplasmic residues, whereas other members of the LytR_cpsA_psr protein family are predicted to have a single transmembrane domain. This unique topology, with the short cytoplasmic domain, membrane localization, and large extracellular domain, suggests a novel mechanism of transcriptional regulation. Therefore, to determine the actual membrane topology of CpsA, specific protein domains were fused to beta-galactosidase or alkaline phosphatase. Enzymatic assays confirmed that the predicted membrane topology for CpsA is correct. To investigate how this integral membrane protein may be functioning in regulation of capsule transcription, purified full-length and truncated forms of CpsA were used in electrophoretic mobility shift assays to characterize the ability to bind the capsule operon promoter. Assays revealed that full-length, purified CpsA protein binds specifically to DNA containing the capsule promoter region. Furthermore, the large extracellular domain is not required for DNA binding, but all cytoplasmic regions of CpsA are necessary and sufficient for specific binding to the capsule operon promoter. This is the first demonstration of a member of this protein family interacting with its target DNA. Taken together, CpsA, as well as other members of the LytR_cpsA_psr protein family, appears to utilize a unique mechanism of transcriptional regulation.

Indexed as

Alkaline PhosphataseBacterial CapsulesBacterial Proteinsbeta-GalactosidaseCell MembraneDNA, BacterialDNA-Binding ProteinsElectrophoretic Mobility Shift AssayGenes, ReporterMembrane ProteinsPromoter Regions, GeneticProtein BindingRecombinant Fusion ProteinsStreptococcusTrans-ActivatorsAlkaline PhosphataseBacterial Proteinsbeta-GalactosidaseDNA, BacterialDNA-Binding ProteinsMembrane ProteinsRecombinant Fusion ProteinsTrans-Activators

Identifiers

PMID21097630
PMCPMC3019820
OpenAlexW2105932887

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.