Pectobacterium atrosepticum KDPG aldolase, Eda, participates in the Entner-Doudoroff pathway and independently inhibits expression of virulence determinants.
Pectobacterium
Eda
Entner-Doudoroff pathway
pathogenicity
Journal
Molecular plant pathology
ISSN: 1364-3703
Titre abrégé: Mol Plant Pathol
Pays: England
ID NLM: 100954969
Informations de publication
Date de publication:
02 2021
02 2021
Historique:
received:
24
09
2020
revised:
04
11
2020
accepted:
04
11
2020
pubmed:
11
12
2020
medline:
18
8
2021
entrez:
10
12
2020
Statut:
ppublish
Résumé
Pectobacterium carotovorum has an incomplete Entner-Doudoroff (ED) pathway, including enzyme 2-keto-3-deoxy-6-phosphogluconate aldolase (Eda) but lacking phosphogluconate dehydratase (Edd), while P. atrosepticum (Pba) has a complete pathway. To understand the role of the ED pathway in Pectobacterium infection, mutants of these two key enzymes, Δeda and Δedd, were constructed in Pba SCRI1039. Δeda exhibited significant decreased virulence on potato tubers and colonization in planta and was greatly attenuated in pectinase activity and the ability to use pectin breakdown products, including polygalacturonic acid (PGA) and galacturonic acid. These reduced phenotypes were restored following complementation with an external vector expressing eda. Quantitative reverse transcription PCR analysis revealed that expression of the pectinase genes pelA, pelC, pehN, pelW, and pmeB in Δeda cultured in pyruvate, with or without PGA, was significantly reduced compared to the wild type, while genes for virulence regulators (kdgR, hexR, hexA, and rsmA) remained unchanged. However, Δedd showed similar phenotypes to the wild type. To our knowledge, this is the first demonstration that disruption of eda has a feedback effect on inhibiting pectin degradation and that Eda is involved in building the arsenal of pectinases needed during infection by Pectobacterium.
Identifiants
pubmed: 33301200
doi: 10.1111/mpp.13025
pmc: PMC7814964
doi:
Substances chimiques
Pectins
89NA02M4RX
Aldehyde-Lyases
EC 4.1.2.-
phospho-2-keto-3-deoxy-gluconate aldolase
EC 4.1.2.14
Hydro-Lyases
EC 4.2.1.-
phosphogluconate dehydratase
EC 4.2.1.12
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
271-283Informations de copyright
© 2020 The Authors. Molecular Plant Pathology published by British Society for Plant Pathology and John Wiley & Sons Ltd.
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