Evidence map›Paper›PMID 25092029›Full record

ArticleJournal of bacteriology2014

Probing the structure of the S105 hole.

Kam H To, Ry Young

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
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  4. Review
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  7. Review
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  9. Pinholin SBiochimica et biophysica acta. Biomembranes · 2021
    Article
  10. Review
  11. Article
  12. Article
  13. Article
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  15. Active SBiochimica et biophysica acta. Biomembranes · 2020
    Article
  16. International journal of molecular sciences · 2020
    Article
  17. Article
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Kam H ToCenter for Phage Technology, Department of Biochemistry and Biophysics, and Department of Biology, Texas A&M University, College Station, Texas, USA.
Ry YoungCenter for Phage Technology, Department of Biochemistry and Biophysics, and Department of Biology, Texas A&M University, College Station, Texas, USA ryland@tamu.edu.
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

For most phages, holins control the timing of host lysis. During the morphogenesis period of the infection cycle, canonical holins accumulate harmlessly in the cytoplasmic membrane until they suddenly trigger to form lethal lesions called holes. The holes can be visualized by cryo-electron microscopy and tomography as micrometer-scale interruptions in the membrane. To explore the fine structure of the holes formed by the lambda holin, S105, a cysteine-scanning accessibility study was performed. A collection of S105 alleles encoding holins with a single Cys residue in different positions was developed and characterized for lytic function. Based on the ability of 4-acetamido-4'-((iodoacetyl) amino) stilbene-2,2'-disulfonic acid, disodium salt (IASD), to modify these Cys residues, one face of transmembrane domain 1 (TMD1) and TMD3 was judged to face the lumen of the S105 hole. In both cases, the lumen-accessible face was found to correspond to the more hydrophilic face of the two TMDs. Judging by the efficiency of IASD modification, it was concluded that the bulk of the S105 protein molecules were involved in facing the lumen. These results are consistent with a model in which the perimeters of the S105 holes are lined by the holin molecules present at the time of lysis. Moreover, the findings that TMD1 and TMD3 face the lumen, coupled with previous results showing TMD2-TMD2 contacts in the S105 dimer, support a model in which membrane depolarization drives the transition of S105 from homotypic to heterotypic oligomeric interactions.

Indexed as

Amino Acid SequenceBacteriophage lambdaCell MembraneEscherichia coliGene Expression Regulation, ViralMolecular Sequence DataViral ProteinsVirus Releasebacteriophage lambda lysis effector protein S105Viral Proteins

Identifiers

PMID25092029
PMCPMC4248806
OpenAlexW2112773023

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.