Evidence map›Paper›PMID 20622018›Full record

ArticleThe Journal of biological chemistry2010

Transcriptomic analyses of xylan degradation by Prevotella bryantii and insights into energy acquisition by xylanolytic bacteroidetes.

Dylan Dodd, Young-Hwan Moon, Kankshita Swaminathan, Roderick I Mackie, Isaac K O Cann

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

65 citing papers in PubMed, 143 citations in OpenAlex.

  1. Article
  2. Article
  3. Food science & nutrition · 2026
    Article
  4. Effects ofAnimals : an open access journal from MDPI · 2026
    Article
  5. Article
  6. Complete genome sequence ofMicrobiology resource announcements · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The catabolic specialization of the marine bacteriumApplied and environmental microbiology · 2024
    Article
  13. Article
  14. HadzaCell reports · 2023
    Article
  15. HadzabioRxiv : the preprint server for biology · 2023
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

5 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 1 country.

Dylan DoddDepartment of Microbiology, University of Illinois, Urbana, Illinois 61801, USA.
Young-Hwan Moon
Kankshita Swaminathan
Roderick I Mackie
Isaac K O Cann
University of Illinois Urbana-Champaign · USEnergy Biosciences Institute · US

Funding

Biochemical Characterization of Specificity for Family 3 Glycoside HydrolasesF30DK084726 · NIDDK · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI DODD, DYLAN · 2009 to 2013
$170k
NIDDK NIH HHS 1F30DK084726NIDDK NIH HHS F30 DK084726
6 · The paper itself

Abstract

Enzymatic depolymerization of lignocellulose by microbes in the bovine rumen and the human colon is critical to gut health and function within the host. Prevotella bryantii B(1)4 is a rumen bacterium that efficiently degrades soluble xylan. To identify the genes harnessed by this bacterium to degrade xylan, the transcriptomes of P. bryantii cultured on either wheat arabinoxylan or a mixture of its monosaccharide components were compared by DNA microarray and RNA sequencing approaches. The most highly induced genes formed a cluster that contained putative outer membrane proteins analogous to the starch utilization system identified in the prominent human gut symbiont Bacteroides thetaiotaomicron. The arrangement of genes in the cluster was highly conserved in other xylanolytic Bacteroidetes, suggesting that the mechanism employed by xylan utilizers in this phylum is conserved. A number of genes encoding proteins with unassigned function were also induced on wheat arabinoxylan. Among these proteins, a hypothetical protein with low similarity to glycoside hydrolases was shown to possess endoxylanase activity and subsequently assigned to glycoside hydrolase family 5. The enzyme was designated PbXyn5A. Two of the most similar proteins to PbXyn5A were hypothetical proteins from human colonic Bacteroides spp., and when expressed each protein exhibited endoxylanase activity. By using site-directed mutagenesis, we identified two amino acid residues that likely serve as the catalytic acid/base and nucleophile as in other GH5 proteins. This study therefore provides insights into capture of energy by xylanolytic Bacteroidetes and the application of their enzymes as a resource in the biofuel industry.

Indexed as

AnimalsBacterial ProteinsBacteroidesCattleColonEndo-1,4-beta XylanasesGene Expression ProfilingGene Expression Regulation, BacterialHumansOligonucleotide Array Sequence AnalysisPrevotellaRumenXylansBacterial ProteinsEndo-1,4-beta XylanasesXylans

Identifiers

PMID20622018
PMCPMC2943253
OpenAlexW2094628495

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.