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Svx Peptidases of Phytopathogenic Pectolytic Bacteria: Structural, Catalytic and Phytoimmune Properties

Tendiuk, Natalia ; Diakonova, Anastasiya ; Petrova, Olga ; Mukhametzyanov, Timur ; Makshakova, Olga ; Gorshkov, Vladimir

International journal of molecular sciences, 2024-01, Vol.25 (2), p.756 [Periódico revisado por pares]

Switzerland: MDPI AG

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Título:
Svx Peptidases of Phytopathogenic Pectolytic Bacteria: Structural, Catalytic and Phytoimmune Properties
Autor: Tendiuk, Natalia ; Diakonova, Anastasiya ; Petrova, Olga ; Mukhametzyanov, Timur ; Makshakova, Olga ; Gorshkov, Vladimir
Assuntos: Amino acids ; Bacteria ; Binding sites ; Biological Assay ; Biological Transport ; Catalysis ; Dickeya ; Ethylenediaminetetraacetic acid ; Genes ; gluzincin extracellular metallopeptidases ; Hydrogen peroxide ; Immune response ; Leaves ; Pathogens ; Pectobacterium ; Peptide Hydrolases ; phytoimmunosuppressors ; plant susceptible responses ; plant-pathogen interactions ; Proteases ; protein structure ; Proteins ; Scientific equipment and supplies industry ; Tobacco ; Virulence ; Virulence (Microbiology)
É parte de: International journal of molecular sciences, 2024-01, Vol.25 (2), p.756
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: Svx proteins are virulence factors secreted by phytopathogenic bacteria of the genus into the host plant cell wall. Svx-encoding genes are present in almost all species of the soft rot Pectobacteriaceae ( and genera). The Svx of ( ) has been shown to be a gluzincin metallopeptidase that presumably targets plant extensins, proteins that contribute to plant cell wall rigidity and participate in cell signaling. However, the particular "output" of the Svx action in terms of plant-pathogen interactions and plant immune responses remained unknown. The Svx proteins are largely unexplored in species, even though some of them have genes encoding two Svx homologs. Therefore, our study aims to compare the structural and catalytic properties of the Svx proteins of and ( ) and to test the phytoimmune properties of these proteins. Two assayed Svx proteins, similar to Svx, were gluzincin metallopeptidases with conservative tertiary structures. The two domains of the Svx proteins form electronegative clefts where the active centers of the peptidase domains are located. All three assayed Svx proteins possessed phytoimmunosuppressory properties and induced ethylene-mediated plant susceptible responses that play a decisive role in -caused disease.
Editor: Switzerland: MDPI AG
Idioma: Inglês

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Svx Peptidases of Phytopathogenic Pectolytic Bacteria: Structural, Catalytic and Phytoimmune Properties

Tendiuk, Natalia ; Diakonova, Anastasiya ; Petrova, Olga ; Mukhametzyanov, Timur ; Makshakova, Olga ; Gorshkov, Vladimir

Switzerland: MDPI AG

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