Evidence map›Paper›PMID 10515910›Full record

ArticleJournal of bacteriology1999

Genetic and biochemical characterization of a high-affinity betaine uptake system (BusA) in Lactococcus lactis reveals a new functional organization within bacterial ABC transporters.

D Obis, A Guillot, J C Gripon, P Renault, A Bolotin, M Y Mistou

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

31 citing papers in PubMed, 95 citations in OpenAlex.

  1. Inactivation of KhpB (EloR/Jag) inApplied and environmental microbiology · 2025
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  2. Review
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  4. Health-Promoting Nature ofFrontiers in microbiology · 2022
    Article
  5. Article
  6. Identification of a GntR family regulator BusRExtremophiles : life under extreme conditions · 2019
    Article
  7. Article
  8. Article
  9. Article
  10. Acid Stress Response Mechanisms of Group B Streptococci.Frontiers in cellular and infection microbiology · 2017
    Review
  11. Stress Physiology of Lactic Acid Bacteria.Microbiology and molecular biology reviews : MMBR · 2016
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

6 authors at 2 institutions in 2 countries.

D ObisUnité de Biochimie et Structure des Protéines, Institut National de la Recherche Agronomique, 78352 Jouy-en-Josas Cedex, France.
A Guillot
J C Gripon
P Renault
A Bolotin
M Y Mistou
Bioénergétique et Ingénierie des Protéines · FRDépartement Génétique Animale · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The cytoplasmic accumulation of exogenous betaine stimulates the growth of Lactococcus lactis cultivated under hyperosmotic conditions. We report that L. lactis possesses a single betaine transport system that belongs to the ATP-binding cassette (ABC) superfamily of transporters. Through transposon mutagenesis, a mutant deficient in betaine transport was isolated. We identified two genes, busAA and busAB, grouped in an operon, busA (betaine uptake system). The transcription of busA is strongly regulated by the external osmolality of the medium. The busAA gene codes for the ATP-binding protein. busAB encodes a 573-residue polypeptide which presents two striking features: (i) a fusion between the regions encoding the transmembrane domain (TMD) and the substrate-binding domain (SBD) and (ii) a swapping of the SBD subdomains when compared to the Bacillus subtilis betaine-binding protein, OpuAC. BusA of L. lactis displays a high affinity towards betaine (K(m) = 1.7 microM) and is an osmosensor whose activity is tightly regulated by external osmolality, leading the betaine uptake capacity of L. lactis to be under dual control at the biochemical and genetic levels. A protein presenting the characteristics predicted for BusAB was detected in the membrane fraction of L. lactis. The fusion between the TMD and the SBD is the first example of a new organization within prokaryotic ABC transporters.

Indexed as

Adenosine TriphosphatasesGenes, BacterialAmino Acid SequenceATP-Binding Cassette TransportersBacterial ProteinsBetaineBiological TransportCell FractionationGene Expression Regulation, BacterialLactococcus lactisMolecular Sequence DataMutagenesis, Site-DirectedOsmotic PressureSequence Analysis, DNASequence Homology, Amino AcidAdenosine TriphosphatasesATP-Binding Cassette TransportersBacterial ProteinsBetaineBusAA protein, Lactococcus lactis

Identifiers

PMID10515910
PMCPMC103755
OpenAlexW2140922812

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.