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Barley RIC157 is involved in RACB-mediated susceptibility to powdery mildew
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Abstract
Successful obligate pathogens benefit from host cellular processes. For the biotrophic ascomycete fungus
Blumeria graminis
f.sp.
hordei
(
Bgh
) it has been shown that barley RACB, a small monomeric G-protein (ROP, RHO of plants), is required for full susceptibility to fungal penetration. The susceptibility function of RACB probably lies in its role in cell polarisation, which may be co-opted by the pathogen for invasive ingrowth of its haustorium. However, the actual mechanism of how RACB supports the fungal penetration success is little understood. RIC proteins (ROP-Interactive and CRIB-(Cdc42/Rac Interactive Binding) motif-containing) are considered scaffold proteins which can interact directly with ROPs via a conserved CRIB motif. Here we describe a yet uncharacterised RIC protein, RIC157, which can interact directly with RACB
in planta
. We show that RIC157 undergoes a recruitment from the cytoplasm to the cell periphery in the presence of activated RACB. During fungal infection, RIC157 and activated RACB colocalise at the penetration site, particularly at the haustorial neck. In a RACB-dependent manner, transiently overexpressed RIC157 renders barley epidermal cells more susceptible to fungal penetration. This suggests that RIC157 promotes fungal penetration into barley epidermal cells via its function downstream of RACB.
Title: Barley RIC157 is involved in RACB-mediated susceptibility to powdery mildew
Description:
Abstract
Successful obligate pathogens benefit from host cellular processes.
For the biotrophic ascomycete fungus
Blumeria graminis
f.
sp.
hordei
(
Bgh
) it has been shown that barley RACB, a small monomeric G-protein (ROP, RHO of plants), is required for full susceptibility to fungal penetration.
The susceptibility function of RACB probably lies in its role in cell polarisation, which may be co-opted by the pathogen for invasive ingrowth of its haustorium.
However, the actual mechanism of how RACB supports the fungal penetration success is little understood.
RIC proteins (ROP-Interactive and CRIB-(Cdc42/Rac Interactive Binding) motif-containing) are considered scaffold proteins which can interact directly with ROPs via a conserved CRIB motif.
Here we describe a yet uncharacterised RIC protein, RIC157, which can interact directly with RACB
in planta
.
We show that RIC157 undergoes a recruitment from the cytoplasm to the cell periphery in the presence of activated RACB.
During fungal infection, RIC157 and activated RACB colocalise at the penetration site, particularly at the haustorial neck.
In a RACB-dependent manner, transiently overexpressed RIC157 renders barley epidermal cells more susceptible to fungal penetration.
This suggests that RIC157 promotes fungal penetration into barley epidermal cells via its function downstream of RACB.
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