Evidence map›Paper›PMID 10850986›Full record

ArticleJournal of bacteriology2000

Characterization of a Snorhizobium meliloti ATP-binding cassette histidine transporter also involved in betaine and proline uptake.

E Boncompagni, L Dupont, T Mignot, M Osteräs, A Lambert, M C Poggi, D Le Rudulier

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

20 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  3. International journal of systematic and evolutionary microbiology · 2021
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  4. Global Metabolomics Reveals ThatFrontiers in bioengineering and biotechnology · 2021
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  9. Mapping the Sinorhizobium meliloti 1021 solute-binding protein-dependent transportome.Proceedings of the National Academy of Sciences of the United States of America · 2006
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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

7 authors at 2 institutions in 1 country.

E BoncompagniLaboratoire de Biologie Végétale et Microbiologie, CNRS ESA 6169, Faculté des Sciences Université de Nice-Sophia Antipolis, Parc Valrose, 06108 Nice Cedex, France.
L Dupont
T Mignot
M Osteräs
A Lambert
M C Poggi
D Le Rudulier
Université Côte d'Azur · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The symbiotic soil bacterium Sinorhizobium meliloti uses the compatible solutes glycine betaine and proline betaine for both protection against osmotic stress and, at low osmolarities, as an energy source. A PCR strategy based on conserved domains in components of the glycine betaine uptake systems from Escherichia coli (ProU) and Bacillus subtilis (OpuA and OpuC) allowed us to identify a highly homologous ATP-binding cassette (ABC) binding protein-dependent transporter in S. meliloti. This system was encoded by three genes (hutXWV) of an operon which also contained a fourth gene (hutH2) encoding a putative histidase, which is an enzyme involved in the first step of histidine catabolism. Site-directed mutagenesis of the gene encoding the periplasmic binding protein (hutX) and of the gene encoding the cytoplasmic ATPase (hutV) was done to study the substrate specificity of this transporter and its contribution in betaine uptake. These mutants showed a 50% reduction in high-affinity uptake of histidine, proline, and proline betaine and about a 30% reduction in low-affinity glycine betaine transport. When histidine was used as a nitrogen source, a 30% inhibition of growth was observed in hut mutants (hutX and hutH2). Expression analysis of the hut operon determined using a hutX-lacZ fusion revealed induction by histidine, but not by salt stress, suggesting this uptake system has a catabolic role rather than being involved in osmoprotection. To our knowledge, Hut is the first characterized histidine ABC transporter also involved in proline and betaine uptake.

Indexed as

Amino Acid Transport SystemsOperonPeriplasmic Binding ProteinsAdenosine TriphosphateAmino Acid SequenceATP-Binding Cassette TransportersBacterial ProteinsBase SequenceBetaineCarrier ProteinsChromosome MappingCloning, MolecularDNA, BacterialHistidineMolecular Sequence DataProlineAdenosine TriphosphateAmino Acid Transport SystemsATP-Binding Cassette TransportersBacterial ProteinsBetaineCarrier ProteinsDNA, BacterialHistidinehistidine-binding proteinPeriplasmic Binding ProteinsProlineProU protein, Bacteria

Identifiers

PMID10850986
PMCPMC94542
OpenAlexW2112150912

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.