Evidence map›Paper›PMID 17056685›Full record

ArticleApplied and environmental microbiology2006

Bioinformatic, genetic, and biochemical evidence that some glycoside hydrolase family 42 beta-galactosidases are arabinogalactan type I oligomer hydrolases.

Stephanie Shipkowski, Jean E Brenchley

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2006. 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
2.2field-weighted citation impact, top 16% 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, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. A Novel Thermal-Activated β-Galactosidase fromFoods (Basel, Switzerland) · 2022
    Article
  5. Article
  6. Review
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  14. Article
  15. Effect of mutations on the thermostability of Aspergillus aculeatus β-1,4-galactanase.Computational and structural biotechnology journal · 2015
    Article
  16. Crystallization and preliminary crystallographic analysis of GanB, a GH42 intracellular β-galactosidase from Geobacillus stearothermophilus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    Article
  17. Article
  18. Bacillus subtilis biofilm induction by plant polysaccharides.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. 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

2 authors at 1 institution in 1 country.

Stephanie ShipkowskiDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, 209 South Frear, University Park, PA 16802, USA. sar242@psualum.com
Jean E Brenchley
Pennsylvania State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycoside hydrolases are organized into glycoside hydrolase families (GHFs) and within this larger group, the beta-galactosidases are members of four families: 1, 2, 35, and 42. Most genes encoding GHF 42 enzymes are from prokaryotes unlikely to encounter lactose, suggesting a different substrate for these enzymes. In search of this substrate, we analyzed genes neighboring GHF 42 genes in databases and detected an arrangement implying that these enzymes might hydrolyze oligosaccharides released by GHF 53 enzymes from arabinogalactan type I, a pectic plant polysaccharide. Because Bacillus subtilis has adjacent GHF 42 and GHF 53 genes, we used it to test the hypothesis that a GHF 42 enzyme (LacA) could act on the oligosaccharides released by a GHF 53 enzyme (GalA) from galactan. We cloned these genes, plus a second GHF 42 gene from B. subtilis, yesZ, into Escherichia coli and demonstrated that cells expressing LacA with GalA gained the ability to use galactan as a carbon source. We constructed B. subtilis mutants and showed that the increased beta-galactosidase activity generated in response to the addition of galactan was eliminated by inactivating lacA or galA but unaffected by the inactivation of yesZ. As further demonstration, we overexpressed the LacA and GalA proteins in E. coli and demonstrated that these enzymes degrade galactan in vitro as assayed by thin-layer chromatography. Our work provides the first in vivo evidence for a function of some GHF 42 beta-galactosidases. Similar functions for other beta-galactosidases in both GHFs 2 and 42 are suggested by genomic data.

Indexed as

Bacillus subtilisBacterial Proteinsbeta-GalactosidaseComputational BiologyEscherichia coliGalactansGlycoside HydrolasesMutationRecombinant ProteinsarabinogalactanBacterial Proteinsbeta-GalactosidaseGalactansGlycoside HydrolasesRecombinant Proteins

Identifiers

PMID17056685
PMCPMC1694227
OpenAlexW1981897593

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.