Farnusch Kaschani

Nov 30, 2024 | nature.com | Pierre Buscaill |Farnusch Kaschani |Markus Kaiser

AbstractMost angiosperm plants recognise the 22-residue flagellin (flg22) epitope in bacterial flagellin via homologs of cell surface receptor FLS2 (flagellin sensitive-2) and mount pattern-triggered immune responses. However, flg22 is buried within the flagellin protein indicating that proteases might be required for flg22 release.

Oct 11, 2024 | nature.com | Pierre Buscaill |Farnusch Kaschani

AbstractRecognizing pathogen-associated molecular patterns on the cell surface is crucial for plant immunity. The proteinaceous nature of many of these patterns suggests that secreted proteases play important roles in their formation and stability. Here we demonstrate that the apoplastic subtilase SBT5.2a inactivates the immunogenicity of cold-shock proteins (CSPs) of the bacterial plant pathogen Pseudomonas syringae by cleaving within the immunogenic csp22 epitope.

Oct 1, 2024 | biorxiv.org | Pierre Buscaill |Nattapong Sanguankiattichai |Farnusch Kaschani |Jie Huang

AbstractMost angiosperm plants recognise the flg22 epitope in bacterial flagellin via homologs of cell surface receptor FLS2 and mount pattern-triggered immune responses. However, flg22 is buried within the flagellin protein indicating that proteases might be required for flg22 release.

May 24, 2024 | biorxiv.org | Pierre Buscaill |Nattapong Sanguankiattichai |Farnusch Kaschani |Jie Huang

AbstractMost angiosperms recognise the flg22 epitope in bacterial flagellin via homologs of cell surface receptor FLS2 and mount pattern-triggered immune responses. However, flg22 is buried within the flagellin protein and logic and preliminary experiments have indicated that proteases might be required for flg22 release. Here, we demonstrate that the extracellular subtilase SBT5.2 processes flg22 from its precursor in the apoplast of Nicotiana benthamiana.

Feb 27, 2024 | nature.com | Matthew Day |Bilal Tetik |Yasser Almeida-Hernandez |Markus Räschle |Farnusch Kaschani |Markus Kaiser | +2 more

AbstractActivation of the replicative Mcm2-7 helicase by loading GINS and Cdc45 is crucial for replication origin firing, and as such for faithful genetic inheritance. Our biochemical and structural studies demonstrate that the helicase activator GINS interacts with TopBP1 through two separate binding surfaces, the first involving a stretch of highly conserved amino acids in the TopBP1-GINI region, the second a surface on TopBP1-BRCT4.