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A family of GHF5 endo-1,4-beta-glucanases in the migratory plant-parasitic nematode Radopholus similis

Annelies Haegeman (UGent) , Joachim Jacob (UGent) , Bartel Vanholme (UGent) , Tina Kyndt (UGent) and Godelieve Gheysen (UGent)
(2008) PLANT PATHOLOGY. 57(3). p.581-590
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Abstract
Endo-1,4-beta-glucanases, which can degrade cellulose, have been identified in a number of plant-parasitic nematodes, mainly sedentary endoparasites. We report the finding of four different endoglucanases of glycosyl hydrolase family 5 (GHF5) in the migratory endoparasitic nematode Radopholus similis. Temporal expression of these genes was analyzed by in situ hybridisation, which showed the presence of transcripts in the pharyngeal gland cells. A semi-quantitative RT-PCR on different developmental stages was done to study the spatial expression pattern. Three of the endoglucanase genes have a reduced expression in adult males as opposed to females. This could be explained by the fact that males do not feed and are considered non-parasitic. Only one of the endoglucanase genes is expressed in juveniles. The four corresponding proteins have a putative signal peptide for secretion and a catalytic domain. Two of the proteins have an additional linker and carbohydrate-binding module (CBM). Modeling of the catalytic domain resulted in the alpha/β-barrel typical for GHF5 endoglucanases. Mapping the conserved amino acids of the four endoglucanases onto the 3D structure revealed that most are positioned near the catalytic centre of the protein, whereas less conserved amino acids occur more often in the alpha helices, pointing towards the outside of the protein. Analyses of the GC contents and codon adaptation indices indicate that the endoglucanase genes are well adapted to the codon usage of Radopholus similis. The GC and GC3 content of the endoglucanases is significantly higher compared to the average for all Radopholus ESTs.
Keywords
GC content, horizontal gene transfer, migratory plant-parasitic nematode, in situ hybridisation, cellulase

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Please use this url to cite or link to this publication:

Chicago
Haegeman, Annelies, Joachim Jacob, Bartel Vanholme, Tina Kyndt, and Godelieve Gheysen. 2008. “A Family of GHF5 Endo-1,4-beta-glucanases in the Migratory Plant-parasitic Nematode Radopholus Similis.” Plant Pathology 57 (3): 581–590.
APA
Haegeman, Annelies, Jacob, J., Vanholme, B., Kyndt, T., & Gheysen, G. (2008). A family of GHF5 endo-1,4-beta-glucanases in the migratory plant-parasitic nematode Radopholus similis. PLANT PATHOLOGY, 57(3), 581–590.
Vancouver
1.
Haegeman A, Jacob J, Vanholme B, Kyndt T, Gheysen G. A family of GHF5 endo-1,4-beta-glucanases in the migratory plant-parasitic nematode Radopholus similis. PLANT PATHOLOGY. Oxford, England: Blackwell; 2008;57(3):581–90.
MLA
Haegeman, Annelies, Joachim Jacob, Bartel Vanholme, et al. “A Family of GHF5 Endo-1,4-beta-glucanases in the Migratory Plant-parasitic Nematode Radopholus Similis.” PLANT PATHOLOGY 57.3 (2008): 581–590. Print.
@article{534407,
  abstract     = {Endo-1,4-beta-glucanases, which can degrade cellulose, have been identified in a number of plant-parasitic nematodes, mainly sedentary endoparasites. We report the finding of four different endoglucanases of glycosyl hydrolase family 5 (GHF5) in the migratory endoparasitic nematode Radopholus similis. Temporal expression of these genes was analyzed by in situ hybridisation, which showed the presence of transcripts in the pharyngeal gland cells. A semi-quantitative RT-PCR on different developmental stages was done to study the spatial expression pattern. Three of the endoglucanase genes have a reduced expression in adult males as opposed to females. This could be explained by the fact that males do not feed and are considered non-parasitic. Only one of the endoglucanase genes is expressed in juveniles. The four corresponding proteins have a putative signal peptide for secretion and a catalytic domain. Two of the proteins have an additional linker and carbohydrate-binding module (CBM). Modeling of the catalytic domain resulted in the alpha/\ensuremath{\beta}-barrel typical for GHF5 endoglucanases. Mapping the conserved amino acids of the four endoglucanases onto the 3D structure revealed that most are positioned near the catalytic centre of the protein, whereas less conserved amino acids occur more often in the alpha helices, pointing towards the outside of the protein. Analyses of the GC contents and codon adaptation indices indicate that the endoglucanase genes are well adapted to the codon usage of Radopholus similis. The GC and GC3 content of the endoglucanases is significantly higher compared to the average for all Radopholus ESTs.},
  author       = {Haegeman, Annelies and Jacob, Joachim and Vanholme, Bartel and Kyndt, Tina and Gheysen, Godelieve},
  issn         = {0032-0862},
  journal      = {PLANT PATHOLOGY},
  keyword      = {GC content,horizontal gene transfer,migratory plant-parasitic nematode,in situ hybridisation,cellulase},
  language     = {eng},
  number       = {3},
  pages        = {581--590},
  publisher    = {Blackwell},
  title        = {A family of GHF5 endo-1,4-beta-glucanases in the migratory plant-parasitic nematode Radopholus similis},
  url          = {http://dx.doi.org/10.1111/j.1365-3059.2007.01814.x},
  volume       = {57},
  year         = {2008},
}

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