Jacobs A

References (3)

Title : A Phelipanche ramosa KAI2 protein perceives strigolactones and isothiocyanates enzymatically - de Saint Germain_2021_Plant.Commun_2_100166
Author(s) : de Saint Germain A , Jacobs A , Brun G , Pouvreau JB , Braem L , Cornu D , Clave G , Baudu E , Steinmetz V , Servajean V , Wicke S , Gevaert K , Simier P , Goormachtig S , Delavault P , Boyer FD
Ref : Plant Commun , 2 :100166 , 2021
Abstract : Phelipanche ramosa is an obligate root-parasitic weed that threatens major crops in central Europe. In order to germinate, it must perceive various structurally divergent host-exuded signals, including isothiocyanates (ITCs) and strigolactones (SLs). However, the receptors involved are still uncharacterized. Here, we identify five putative SL receptors in P. ramosa and show that PrKAI2d3 is involved in the stimulation of seed germination. We demonstrate the high plasticity of PrKAI2d3, which allows it to interact with different chemicals, including ITCs. The SL perception mechanism of PrKAI2d3 is similar to that of endogenous SLs in non-parasitic plants. We provide evidence that PrKAI2d3 enzymatic activity confers hypersensitivity to SLs. Additionally, we demonstrate that methylbutenolide-OH binds PrKAI2d3 and stimulates P. ramosa germination with bioactivity comparable to that of ITCs. This study demonstrates that P. ramosa has extended its signal perception system during evolution, a fact that should be considered for the development of specific and efficient biocontrol methods.
ESTHER : de Saint Germain_2021_Plant.Commun_2_100166
PubMedSearch : de Saint Germain_2021_Plant.Commun_2_100166
PubMedID: 34746757
Gene_locus related to this paper: phera-PrKAI2c , phera-PrKAI2d1 , phera-PrKAI2d2 , phera-PrKAI2d3 , phera-PrKAI2d4

Title : Unraveling the MAX2 Protein Network in Arabidopsis thaliana: Identification of the Protein Phosphatase PAPP5 as a Novel MAX2 Interactor - Struk_2020_Mol.Cell.Proteomics__
Author(s) : Struk S , De Cuyper C , Jacobs A , Braem L , Walton A , De Keyser A , Depuydt S , Vu LD , De Smet I , Boyer FD , Eeckhout D , Persiau G , Gevaert K , De Jaeger G , Goormachtig S
Ref : Mol Cell Proteomics , : , 2020
Abstract : The F-box protein MORE AXILLARY GROWTH 2 (MAX2) is a central component in the signaling cascade of strigolactones (SLs) as well as of the smoke derived karrikins (KARs) and the so far unknown endogenous KAI2 ligand (KL). The two groups of molecules are involved in overlapping and unique developmental processes, and signal-specific outcomes are attributed to perception by the paralogous alpha/beta-hydrolases DWARF14 (D14) for SL and KARRIKIN INSENSITIVE 2/ HYPOSENSITIVE TO LIGHT (KAI2/HTL) for KAR/KL. Additionally, depending on which receptor is activated, specific members of the SUPPRESSOR OF MAX2 1 (SMAX1) - LIKE (SMXL) family control KAR/KL and SL responses. As proteins that function in the same signal transduction pathway often occur in large protein complexes, we aimed at discovering new players of the MAX2, D14 and KAI2 protein network by tandem affinity purification using Arabidopsis cell cultures. When using MAX2 as a bait, various proteins were co-purified among which general components of the Skp1-Cullin-F-box complex and members of the CONSTITUTIVE PHOTOMORPHOGENIC 9 signalosome. Here, we report the identification of a novel interactor of MAX2, a type 5 serine/threonine protein phosphatase, designated PHYTOCHROME-ASSOCIATED PROTEIN PHOSPHATASE 5 (PAPP5). Quantitative affinity purification pointed at PAPP5 as being more present in KAI2 rather than D14 protein complexes. In agreement, mutant analysis suggests that PAPP5 modulates KAR/KL-dependent seed germination in suboptimal conditions and seedling development. Additionally, a phosphopeptide enrichment experiment revealed that PAPP5 might dephosphorylate MAX2 in vivo independently of the synthetic strigolactone analog, rac-GR24. Together, by analyzing the protein complexes to which MAX2, D14 and KAI2 belong, we revealed a new MAX2 interactor, PAPP5, that might act through dephosphorylation of MAX2 to control mainly KAR/KL- related phenotypes and, hence, provide another link with the light pathway.
ESTHER : Struk_2020_Mol.Cell.Proteomics__
PubMedSearch : Struk_2020_Mol.Cell.Proteomics__
PubMedID: 33372050

Title : A Phelipanche ramosa KAI2 Protein Perceives enzymatically Strigolactones and Isothiocyanates - de Saint Germain_2020_Biorxiv__
Author(s) : de Saint Germain A , Jacobs A , Brun G , Pouvreau JB , Braem L , Cornu D , Clave G , Baudu E , Steinmetz V , Servajean V , Wicke S , Gevaert K , Simier P , Goormachti S , Delavault P , Boyer FD
Ref : Biorxiv , : , 2020
Abstract : Phelipanche ramosa is an obligate root-parasitic weed threatening major crops in central Europe. For its germination, it has to perceive various structurally diverging host-exuded signals, including isothiocyanates (ITCs) and strigolactones (SLs). However, the receptors involved are still uncharacterized. Here, we identified five putative SL receptors in P. ramosa, of which PrKAI2d3 is involved in seed germination stimulation. We established the high plasticity of PrKAI2d3, allowing interaction with different chemicals, including ITCs. The SL perception mechanism of PrKAI2d3 is similar to that of endogenous SLs in non-parasitic plants. We provide evidence that the PrKAI2d3 enzymatic activity confers hypersensitivity to SLs. Additionally, we demonstrated that methylbutenolide-OH binds PrKAI2d3 and stimulates P. ramosa germination with a bioactivity comparable to that of ITCs. This study highlights that P. ramosa has extended its signal perception system during evolution, a fact to be considered in the development of specific and efficient biocontrol methods.
ESTHER : de Saint Germain_2020_Biorxiv__
PubMedSearch : de Saint Germain_2020_Biorxiv__
PubMedID: