Evidence map›Paper›PMID 25266726›Full record

ArticleThe Journal of biological chemistry2014

Molecular mechanisms associated with xylan degradation by Xanthomonas plant pathogens.

Camila Ramos Santos, Zaira Bruna Hoffmam, Vanesa Peixoto de Matos Martins, Leticia Maria Zanphorlin, Leandro Henrique de Paula Assis, Rodrigo Vargas Honorato, Paulo Sérgio Lopes de Oliveira, Roberto Ruller, Mario Tyago Murakami

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.3field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
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  12. The catabolic specialization of the marine bacteriumApplied and environmental microbiology · 2024
    Article
  13. Endophytic non-pathogenicFrontiers in plant science · 2024
    Article
  14. Xylose Isomerase Depletion Enhances Virulence ofInternational journal of molecular sciences · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
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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

9 authors at 2 institutions in 1 country.

Camila Ramos SantosBiosciences National Laboratory and National Center for Research in Energy and Materials, Campinas, São Paulo, 13083-970, Brazil.
Zaira Bruna HoffmamBioethanol Science and Technology Laboratory, National Center for Research in Energy and Materials, Campinas, São Paulo, 13083-970, Brazil.
Vanesa Peixoto de Matos MartinsBiosciences National Laboratory and National Center for Research in Energy and Materials, Campinas, São Paulo, 13083-970, Brazil.
Leticia Maria ZanphorlinBioethanol Science and Technology Laboratory, National Center for Research in Energy and Materials, Campinas, São Paulo, 13083-970, Brazil.
Leandro Henrique de Paula AssisBiosciences National Laboratory and National Center for Research in Energy and Materials, Campinas, São Paulo, 13083-970, Brazil.
Rodrigo Vargas HonoratoBiosciences National Laboratory and National Center for Research in Energy and Materials, Campinas, São Paulo, 13083-970, Brazil.
Paulo Sérgio Lopes de OliveiraBiosciences National Laboratory and National Center for Research in Energy and Materials, Campinas, São Paulo, 13083-970, Brazil.
Roberto RullerBioethanol Science and Technology Laboratory, National Center for Research in Energy and Materials, Campinas, São Paulo, 13083-970, Brazil.
Mario Tyago MurakamiBiosciences National Laboratory and National Center for Research in Energy and Materials, Campinas, São Paulo, 13083-970, Brazil. Electronic address: mario.murakami@lnbio.cnpem.br.
Brazilian Biosciences National Laboratory · BRBrazilian Center for Research in Energy and Materials · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Xanthomonas pathogens attack a variety of economically relevant plants, and their xylan CUT system (carbohydrate utilization with TonB-dependent outer membrane transporter system) contains two major xylanase-related genes, xynA and xynB, which influence biofilm formation and virulence by molecular mechanisms that are still elusive. Herein, we demonstrated that XynA is a rare reducing end xylose-releasing exo-oligoxylanase and not an endo-β-1,4-xylanase as predicted. Structural analysis revealed that an insertion in the β7-α7 loop induces dimerization and promotes a physical barrier at the +2 subsite conferring this unique mode of action within the GH10 family. A single mutation that impaired dimerization became XynA active against xylan, and high endolytic activity was achieved when this loop was tailored to match a canonical sequence of endo-β-1,4-xylanases, supporting our mechanistic model. On the other hand, the divergent XynB proved to be a classical endo-β-1,4-xylanase, despite the low sequence similarity to characterized GH10 xylanases. Interestingly, this enzyme contains a calcium ion bound nearby to the glycone-binding region, which is required for catalytic activity and structural stability. These results shed light on the molecular basis for xylan degradation by Xanthomonas and suggest how these enzymes synergistically assist infection and pathogenesis. Our findings indicate that XynB contributes to breach the plant cell wall barrier, providing nutrients and facilitating the translocation of effector molecules, whereas the exo-oligoxylanase XynA possibly participates in the suppression of oligosaccharide-induced immune responses.

Indexed as

Amino Acid SequenceBacterial Proteinsbeta-GlucosidaseCalciumCalorimetryCarbohydrate MetabolismCell WallCloning, MolecularCrystallography, X-RayEndo-1,4-beta XylanasesGlycoside HydrolasesIonsMolecular Sequence DataOligosaccharidesPlantsProtein EngineeringBacterial Proteinsbeta-GlucosidaseCalciumEndo-1,4-beta XylanasesGlycoside HydrolasesIonsOligosaccharidesXylansXynB xylanaseBiotechnologyCell Wall-degrading EnzymesCrystal StructureEnzyme KineticsGH10 FamilyGlycoside HydrolaseProtein EngineeringXanthomonas axonopodis pv. citriXylan CUT System

Identifiers

PMID25266726
PMCPMC4231694
OpenAlexW1978430903

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.