Evidence map›Paper›PMID 10869078›Full record

ArticleJournal of bacteriology2000

A novel bacterial ATP-binding cassette transporter system that allows uptake of macromolecules.

K Momma, M Okamoto, Y Mishima, S Mori, W Hashimoto, K Murata

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 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.4field-weighted citation impact, top 11% 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, 78 citations in OpenAlex.

  1. Three alginate lyases provide a new gutApplied and environmental microbiology · 2023
    Article
  2. Article
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  4. 4-Deoxy-l-Molecules (Basel, Switzerland) · 2022
    Review
  5. Bacteria with a mouth: Discovery and new insights into cell surface structure and macromolecule transport.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2022
    Article
  6. Review
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  18. Crystallization and preliminary X-ray analysis of alginate importer from Sphingomonas sp. A1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
  19. Crystallization and preliminary crystallographic analysis of the cell-surface alginate-binding protein Algp7 isolated from Sphingomonas sp. A1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009
    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

6 authors at 2 institutions in 1 country.

K MommaResearch Institute for Food Science, Kyoto University, Japan. momma@food2.food.kyoto-u.ac.jp
M Okamoto
Y Mishima
S Mori
W Hashimoto
K Murata
Kyoto Bunkyo University · JPKyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A gram-negative bacterium, Sphingomonas sp. strain A1, isolated as a producer of alginate lyase, has a characteristic cell envelope structure and forms a mouth-like pit on its surface. The pit is produced only when the cells have to incorporate and assimilate alginate. An alginate uptake-deficient mutant was derived from cells of strain A1. One open reading frame, algS (1,089 bp), exhibiting homology to the bacterial ATP-binding domain of an ABC transporter, was cloned as a fragment complementing the mutation. algS was followed by two open reading frames, algM1 (972 bp) and algM2 (879 bp), which exhibit homology with the transmembrane permeases of ABC transporters. Disruption of algS of strain A1 resulted in the failure to incorporate alginate and to form a pit. Hexahistidine-tagged AlgS protein (AlgS(His6)) overexpressed in Escherichia coli and purified by Ni(2+) affinity column chromatography showed ATPase activity. Based on these results, we propose the occurrence of a novel pit-dependent ABC transporter system that allows the uptake of macromolecules.

Indexed as

Bacterial ProteinsAdenosine TriphosphatasesAlginatesATP-Binding Cassette TransportersBiological TransportCloning, MolecularGenetic Complementation TestGlucuronic AcidHexuronic AcidsModels, GeneticModels, StructuralMolecular Sequence DataMutationOpen Reading FramesPolysaccharide-LyasesSequence Analysis, DNAAdenosine TriphosphatasesAlginatesAlgS protein, SphingomonasATP-Binding Cassette TransportersBacterial ProteinsGlucuronic AcidHexuronic Acidspoly(beta-D-mannuronate) lyasePolysaccharide-Lyases

Identifiers

PMID10869078
PMCPMC94585
OpenAlexW2144149845

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.