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- aggregation1
- disease resistance1
- enzyme inhibitor1
- folate1
- GH281
- Glycine max1
- herbivorous insect1
- host-pathogen interaction1
- insect1
- ligand-binding protein1
- LRR protein1
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- polygalacturonase1
- polygalacturonase-inhibiting protein1
- protein aggregation1
- quantitative trait loci (QTL)1
- serine hydroxymethyltransferase 8 (SHMT8)1
- soybean cyst nematode1
- X-ray crystallography1
Plant Biology
2 Results
- Plant BiologyOpen Access
Direct evidence for a new mode of plant defense against insects via a novel polygalacturonase-inhibiting protein expression strategy
Journal of Biological ChemistryVol. 295Issue 33p11833–11844Published online: July 1, 2020- Wiebke Haeger
- Jana Henning
- David G. Heckel
- Yannick Pauchet
- Roy Kirsch
Cited in Scopus: 13Plant cell wall–associated polygalacturonase-inhibiting proteins (PGIPs) are widely distributed in the plant kingdom. They play a crucial role in plant defense against phytopathogens by inhibiting microbial polygalacturonases (PGs). PGs hydrolyze the cell wall polysaccharide pectin and are among the first enzymes to be secreted during plant infection. Recent studies demonstrated that herbivorous insects express their own PG multi-gene families, raising the question whether PGIPs also inhibit insect PGs and protect plants from herbivores. - Protein Structure and FoldingOpen Access
Impaired folate binding of serine hydroxymethyltransferase 8 from soybean underlies resistance to the soybean cyst nematode
Journal of Biological ChemistryVol. 295Issue 11p3708–3718Published online: February 2, 2020- David A. Korasick
- Pramod K. Kandoth
- John J. Tanner
- Melissa G. Mitchum
- Lesa J. Beamer
Cited in Scopus: 6Management of the agricultural pathogen soybean cyst nematode (SCN) relies on the use of SCN-resistant soybean cultivars, a strategy that has been failing in recent years. An underutilized source of resistance in the soybean genotype Peking is linked to two polymorphisms in serine hydroxy-methyltransferase 8 (SHMT8). SHMT is a pyridoxal 5′-phosphate–dependent enzyme that converts l-serine and (6S)-tetrahydrofolate to glycine and 5,10-methylenetetrahydrofolate. Here, we determined five crystal structures of the 1884-residue SHMT8 tetramers from the SCN-susceptible cultivar (cv.) Essex and the SCN-resistant cv.