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The N-Glycan Cluster from Xanthomonas campestris pv. campestris: A toolbox for sequential plant n-glycan processing
- Source :
- Journal of Biological Chemistry 10 (290), 6022-36. (2015), Journal of Biological Chemistry, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (10), pp.6022-36. ⟨10.1074/jbc.M114.624593⟩
- Publication Year :
- 2015
-
Abstract
- International audience; N-Glycans are widely distributed in living organisms but represent only a small fraction of the carbohydrates found in plants. This probably explains why they have not previously been considered as substrates exploited by phytopathogenic bacteria during plant infection. Xanthomonas campestris pv. campestris, the causal agent of black rot disease of Brassica plants, possesses a specific system for GlcNAc utilization expressed during host plant infection. This system encompasses a cluster of eight genes (nixE to nixL) encoding glycoside hydrolases (GHs). In this paper, we have characterized the enzymatic activities of these GHs and demonstrated their involvement in sequential degradation of a plant N-glycan using a N-glycopeptide containing two GlcNAcs, three mannoses, one fucose, and one xylose (N2M3FX) as a substrate. The removal of the α-1,3-mannose by the α-mannosidase NixK (GH92) is a prerequisite for the subsequent action of the β-xylosidase NixI (GH3), which is involved in the cleavage of the β-1,2-xylose, followed by the α-mannosidase NixJ (GH125), which removes the α-1,6-mannose. These data, combined to the subcellular localization of the enzymes, allowed us to propose a model of N-glycopeptide processing by X. campestris pv. campestris. This study constitutes the first evidence suggesting N-glycan degradation by a plant pathogen, a feature shared with human pathogenic bacteria. Plant N-glycans should therefore be included in the repertoire of molecules putatively metabolized by phytopathogenic bacteria during their life cycle.
- Subjects :
- Enzyme Kinetics
Xanthomonas
Glycoside Hydrolases
Bacteria
N-Linked Glycosylation
[SDV]Life Sciences [q-bio]
Glycoside Hydrolase
food and beverages
Brassica
Plant
Xanthomonas campestris
Carbohydrate Processing
Phytopathogen
Xylosidases
Polysaccharides
alpha-Mannosidase
Enzymology
bacteria
Humans
[SDV.BV]Life Sciences [q-bio]/Vegetal Biology
hormones, hormone substitutes, and hormone antagonists
Plant Diseases
Subjects
Details
- Language :
- English
- ISSN :
- 00219258 and 1083351X
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry 10 (290), 6022-36. (2015), Journal of Biological Chemistry, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (10), pp.6022-36. ⟨10.1074/jbc.M114.624593⟩
- Accession number :
- edsair.pmid.dedup....f0a855a165b4caab2ee6ca90969b8069