Evidence map›Paper›PMID 23387988›Full record

ArticleMolecular microbiology2013

Spanin function requires subunit homodimerization through intermolecular disulfide bonds.

Joel D Berry, Manoj Rajaure, Ry Young

Abstract read
In one paragraph

Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
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

30 citing papers in PubMed.

  1. Article
  2. The Lysis cassette of jumbophage PhiKZ.Scientific reports · 2026
    Article
  3. The Lysis Cassette of Jumbophage phiKZ.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Review
  6. Identifying components of theJournal of bacteriology · 2024
    Article
  7. Genome characterization of a multi-drug resistantFrontiers in microbiology · 2024
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Phage Lysis: Multiple Genes for Multiple Barriers.Advances in virus research · 2019
    Review
  18. Article
  19. Article
  20. Viruses · 2018
    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

3 authors.

Joel D BerryCenter for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, USA.
Manoj Rajaure
Ry Young

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 λ Rz and Rz1 proteins are the subunits of the spanin complex, required for the disruption of the outer membrane during host lysis. Rz, the inner membrane or i-spanin, has a largely alpha-helical periplasmic domain, whereas Rz1, the outer membrane or o-spanin, has a 25% proline content with no predicted secondary structure. We report that both Rz and Rz1 accumulate as homodimers covalently linked by intermolecular disulfide bonds involving all three Cys residues, two in Rz and one in Rz1. Moreover, of these three intermolecular disulfides, spanin function requires the presence of at least one of the two linkages nearest the Rz-Rz1 C-terminal interaction domains; i.e. either the Rz1-Rz1 disulfide or the distal Rz-Rz disulfide link. In a dsbC host, but not in dsbA or dsbA dsbC hosts, formation of the covalent homodimers of Rz is severely reduced and outer membrane disruption is significantly delayed, suggesting that the spanin pathway normally proceeds through DsbA-mediated formation of an intramolecular disulfide in Rz. In contrast, efficient formation of the Rz1-Rz1 disulfide requires DsbA. Finally, Dsb-independent formation of the covalent homodimer of either subunit requires the presence of the other, presumably as a template for close apposition of the thiols.

Indexed as

Protein MultimerizationAllelesAmino Acid SequenceAmino Acid SubstitutionBacteriolysisBacteriophage lambdaCysteineDisulfidesKineticsModels, BiologicalMolecular Sequence DataMutant ProteinsMutationPhenotypeProtein SubunitsViral ProteinsCysteineDisulfidesMutant ProteinsProtein SubunitsViral Proteins

Identifiers

PMID23387988
PMCPMC3612274

What OpenQuestion holds

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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.