Structure-Function Characterisation of Eop1 Effectors from the Erwinia-Pantoea Clade Reveals They May Acetylate Their Defence Target through a Catalytic Dyad.

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dc.citation.issue19
dc.citation.volume24
dc.contributor.authorTomar V
dc.contributor.authorRikkerink EHA
dc.contributor.authorSong J
dc.contributor.authorSofkova-Bobcheva S
dc.contributor.authorBus VGM
dc.contributor.editorBhadauria V
dc.contributor.editorZhao W
dc.coverage.spatialSwitzerland
dc.date.accessioned2024-07-17T02:59:02Z
dc.date.available2024-07-17T02:59:02Z
dc.date.issued2023-09-28
dc.description.abstractThe YopJ group of acetylating effectors from phytopathogens of the genera Pseudomonas and Ralstonia have been widely studied to understand how they modify and suppress their host defence targets. In contrast, studies on a related group of effectors, the Eop1 group, lag far behind. Members of the Eop1 group are widely present in the Erwinia-Pantoea clade of Gram-negative bacteria, which contains phytopathogens, non-pathogens and potential biocontrol agents, implying that they may play an important role in agroecological or pathological adaptations. The lack of research in this group of YopJ effectors has left a significant knowledge gap in their functioning and role. For the first time, we perform a comparative analysis combining AlphaFold modelling, in planta transient expressions and targeted mutational analyses of the Eop1 group effectors from the Erwinia-Pantoea clade, to help elucidate their likely activity and mechanism(s). This integrated study revealed several new findings, including putative binding sites for inositol hexakisphosphate and acetyl coenzyme A and newly postulated target-binding domains, and raises questions about whether these effectors function through a catalytic triad mechanism. The results imply that some Eop1s may use a catalytic dyad acetylation mechanism that we found could be promoted by the electronegative environment around the active site.
dc.description.confidentialfalse
dc.edition.editionOctober-1 2023
dc.format.pagination14664-
dc.identifier.author-urlhttps://www.ncbi.nlm.nih.gov/pubmed/37834112
dc.identifier.citationTomar V, Rikkerink EHA, Song J, Sofkova-Bobcheva S, Bus VGM. (2023). Structure-Function Characterisation of Eop1 Effectors from the Erwinia-Pantoea Clade Reveals They May Acetylate Their Defence Target through a Catalytic Dyad.. Int J Mol Sci. 24. 19. (pp. 14664-).
dc.identifier.doi10.3390/ijms241914664
dc.identifier.eissn1422-0067
dc.identifier.elements-typejournal-article
dc.identifier.issn1661-6596
dc.identifier.number14664
dc.identifier.piiijms241914664
dc.identifier.urihttps://mro.massey.ac.nz/handle/10179/70211
dc.languageeng
dc.publisherMDPI (Basel, Switzerland)
dc.publisher.urihttps://www.mdpi.com/1422-0067/24/19/14664
dc.relation.isPartOfInt J Mol Sci
dc.rights(c) 2023 The Author/s
dc.rightsCC BY 4.0
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectAlphaFold models
dc.subjectEop1
dc.subjectErwinia amylovora
dc.subjectYopJ
dc.subjectacetylation
dc.subjectcatalytic dyad
dc.subjecteffector
dc.subjectfire blight
dc.subjectErwinia
dc.subjectPantoea
dc.subjectPseudomonas
dc.subjectDickeya
dc.subjectAcetyl Coenzyme A
dc.subjectPlant Diseases
dc.subjectErwinia amylovora
dc.titleStructure-Function Characterisation of Eop1 Effectors from the Erwinia-Pantoea Clade Reveals They May Acetylate Their Defence Target through a Catalytic Dyad.
dc.typeJournal article
pubs.elements-id480995
pubs.organisational-groupCollege of Health
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