Xyloglucan endotransglycosylase/hydrolase increases tightly-bound xyloglucan and chain number but decreases chain length contributing to the defense response that Glycine max has to Heterodera glycines.
Animals
Chromatography, Gel
Female
Genotype
Glucans
/ chemistry
Glycosyltransferases
/ antagonists & inhibitors
Host-Parasite Interactions
Molecular Weight
Plant Proteins
/ metabolism
Plant Roots
/ parasitology
Plants, Genetically Modified
/ enzymology
Principal Component Analysis
RNA Interference
RNA, Small Interfering
/ metabolism
Glycine max
/ enzymology
Tylenchida
/ physiology
Xylans
/ chemistry
Journal
PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081
Informations de publication
Date de publication:
2021
2021
Historique:
received:
27
10
2020
accepted:
07
12
2020
entrez:
14
1
2021
pubmed:
15
1
2021
medline:
23
4
2021
Statut:
epublish
Résumé
The Glycine max xyloglucan endotransglycosylase/hydrolase (EC 2.4.1.207), GmXTH43, has been identified through RNA sequencing of RNA isolated through laser microdissection of Heterodera glycines-parasitized root cells (syncytia) undergoing the process of defense. Experiments reveal that genetically increasing XTH43 transcript abundance in the H. glycines-susceptible genotype G. max[Williams 82/PI 518671] decreases parasitism. Experiments presented here show decreasing XTH43 transcript abundance through RNA interference (RNAi) in the H. glycines-resistant G. max[Peking/PI 548402] increases susceptibility, but it is unclear what role XTH43 performs. The experiments presented here show XTH43 overexpression decreases the relative length of xyloglucan (XyG) chains, however, there is an increase in the amount of those shorter chains. In contrast, XTH43 RNAi increases XyG chain length. The experiments show that XTH43 has the capability to function, when increased in its expression, to limit XyG chain extension. This outcome would likely impair the ability of the cell wall to expand. Consequently, XTH43 could provide an enzymatically-driven capability to the cell that would allow it to limit the ability of parasitic nematodes like H. glycines to develop a feeding structure that, otherwise, would facilitate parasitism. The experiments presented here provide experimentally-based proof that XTHs can function in ways that could be viewed as being able to limit the expansion of the cell wall.
Identifiants
pubmed: 33444331
doi: 10.1371/journal.pone.0244305
pii: PONE-D-20-33783
pmc: PMC7808671
doi:
Substances chimiques
Glucans
0
Plant Proteins
0
RNA, Small Interfering
0
Xylans
0
xyloglucan
37294-28-3
Glycosyltransferases
EC 2.4.-
xyloglucan endotransglycosylase
EC 2.4.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0244305Déclaration de conflit d'intérêts
The authors have declared that no competing interests exist.
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