Abstract
Two pectate lyase genes (Bx-pel-1 and Bx-pel-2) were cloned from the pine wood nematode, Bursaphelenchus xylophilus. The deduced amino acid sequences of these pectate lyases are most similar to polysaccharide lyase family 3 proteins. Recombinant BxPEL1 showed highest activity on polygalacturonic acid and lower activity on more highly methylated pectin. Recombinant BxPEL1 demonstrated full dependency on Ca2+ for activity and optimal activity at 55 degrees C and pH 8 to 10 like other pectate lyases of polysaccharide lyase family 3. The protein sequences have predicted signal peptides at their N-termini and the genes are expressed solely in the esophageal gland cells of the nematode, indicating that the pectate lyases could be secreted into plant tissues to help feeding and migration in the tree. This study suggests that pectate Iyases are widely distributed in plant-parasitic nematodes and play an important role in plant-nematode interactions.
| Original language | English |
|---|---|
| Pages (from-to) | 280-287 |
| Number of pages | 8 |
| Journal | Molecular Plant-Microbe Interactions |
| Volume | 19 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Mar 2006 |
Keywords
- horizontal gene transfer
- MELOIDOGYNE-INCOGNITA
- ERWINIA-CHRYSANTHEMI
- HETERODERA-GLYCINES
- SEQUENCE ALIGNMENT
- CELL WALLS
- PECTIN
- GENES
- CLASSIFICATION
- DEGRADATION
- CELLULASES