Evidence map›Paper›PMID 16461639›Full record

ArticleApplied and environmental microbiology2006

Identification of an endo-beta-1,4-D-xylanase from Magnaporthe grisea by gene knockout analysis, purification, and heterologous expression.

Sheng-Cheng Wu, Jeffrey E Halley, Christopher Luttig, Linda M Fernekes, Gerardo Gutiérrez-Sanchez, Alan G Darvill, Peter Albersheim

Open access · greenAbstract 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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
5.2field-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

19 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Article
  3. Journal of fungi (Basel, Switzerland) · 2021
    Article
  4. Article
  5. Global Characterization of GH10 Family Xylanase Genes inInternational journal of molecular sciences · 2020
    Article
  6. Article
  7. Deletion of Endo-β-1,4-XylanaseFrontiers in plant science · 2018
    Article
  8. Article
  9. 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

7 authors at 1 institution in 1 country.

Sheng-Cheng WuComplex Carbohydrate Research Center, University of Georgia, 315 Riverbend Rd., Athens, GA 30602-4712, USA. wusc@ccrc.uga.edu
Jeffrey E Halley
Christopher Luttig
Linda M Fernekes
Gerardo Gutiérrez-Sanchez
Alan G Darvill
Peter Albersheim
University of Georgia · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Magnaporthe grisea, a destructive ascomycetous pathogen of rice, secretes cell wall-degrading enzymes into a culture medium containing purified rice cell walls as the sole carbon source. From M. grisea grown under the culture conditions described here, we have identified an expressed sequenced tag, XYL-6, a gene that is also expressed in M. grisea-infected rice leaves 24 h postinoculation with conidia. This gene encodes a protein about 65% similar to endo-beta-1,4-D-glycanases within glycoside hydrolase family GH10. A M. grisea knockout mutant for XYL-6 was created, and it was shown to be as virulent as the parent strain in infecting the rice host. The proteins secreted by the parent strain and by the xyl-6Delta mutant were each fractionated by liquid chromatography, and the collected fractions were assayed for endo-beta-1,4-D-glucanase or endo-beta-1,4-D-xylanase activities. Two protein-containing peaks with endo-beta-1,4-D-xylanase activity secreted by the parent strain are not detectable in the column eluant of the proteins secreted by the mutant. The two endoxylanases (XYL-6alpha and XYL-6beta) from the parent were each purified to homogeneity. N-terminal amino acid sequencing indicated that XYL-6alpha is a fragment of XYL-6beta and that XYL-6beta is identical to the deduced protein sequence encoded by the XYL-6 gene. Finally, XYL-6 was introduced into Pichia pastoris for heterologous expression, which resulted in the purification of a fusion protein, XYL-6H, from the Pichia pastoris culture filtrate. XYL-6H is active in cleaving arabinoxylan. These experiments unequivocally established that the XYL-6 gene encodes a secreted endo-beta-1,4-D-xylanase.

Indexed as

Amino Acid SequenceBase SequenceDNA, ComplementaryDNA, FungalEndo-1,4-beta XylanasesExpressed Sequence TagsGene ExpressionGenes, FungalGene TargetingMagnaportheMolecular Sequence DataMutationOryzaRecombinant Fusion ProteinsSequence Homology, Amino AcidDNA, ComplementaryDNA, FungalEndo-1,4-beta XylanasesRecombinant Fusion Proteins

Identifiers

PMID16461639
PMCPMC1392926
OpenAlexW2172126041

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.