Evidence map›Paper›PMID 23836870›Full record

ArticleJournal of bacteriology2013

Solitary BioY proteins mediate biotin transport into recombinant Escherichia coli.

Friedrich Finkenwirth, Franziska Kirsch, Thomas Eitinger

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2013. 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
2.1field-weighted citation impact, top 15% 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, 42 citations in OpenAlex.

  1. Exploring the Link Between Biotin Metabolism andPathogens (Basel, Switzerland) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The Influence of Genes on the "Killer Plasmid" ofFrontiers in microbiology · 2021
    Article
  7. Comparative genomics of the genusMicrobial genomics · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Structure of a pantothenate transporter and implications for ECF module sharing and energy coupling of group II ECF transporters.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  19. Article
  20. EnterohemorrhagicGut microbes
    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 at 1 institution in 1 country.

Friedrich FinkenwirthInstitut für Biologie/Mikrobiologie, Humboldt-Universität zu Berlin, Berlin, Germany.
Franziska Kirsch
Thomas Eitinger
Humboldt-Universität zu Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Energy-coupling factor (ECF) transporters form a large group of vitamin uptake systems in prokaryotes. They are composed of highly diverse, substrate-specific, transmembrane proteins (S units), a ubiquitous transmembrane protein (T unit), and homo- or hetero-oligomeric ABC ATPases. Biotin transporters represent a special case of ECF-type systems. The majority of the biotin-specific S units (BioY) is known or predicted to interact with T units and ABC ATPases. About one-third of BioY proteins, however, are encoded in organisms lacking any recognizable T unit. This finding raises the question of whether these BioYs function as transporters in a solitary state, a feature ascribed to certain BioYs in the past. To address this question in living cells, an Escherichia coli K-12 derivative deficient in biotin synthesis and devoid of its endogenous high-affinity biotin transporter was constructed as a reference strain. This organism is particularly suited for this purpose because components of ECF transporters do not naturally occur in E. coli K-12. The double mutant was viable in media containing either high levels of biotin or a precursor of the downstream biosynthetic path. Importantly, it was nonviable on trace levels of biotin. Eight solitary bioY genes of proteobacterial origin were individually expressed in the reference strain. Each of the BioYs conferred biotin uptake activity on the recombinants, which was inferred from uptake assays with [(3)H]biotin and growth of the cells on trace levels of biotin. The results underscore that solitary BioY transports biotin across the cytoplasmic membrane.

Indexed as

Biological Transport, ActiveRecombination, GeneticAdenosine TriphosphatasesATP-Binding Cassette TransportersBiotinEscherichia coli K12Escherichia coli ProteinsMembrane Transport ProteinsMutationAdenosine TriphosphatasesATP-Binding Cassette TransportersbioH protein, E coliBiotinEscherichia coli ProteinsMembrane Transport Proteins

Identifiers

PMID23836870
PMCPMC3754743
OpenAlexW2041878149

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.