%0 Journal Article %A Boyle, Patrick %A Schwizer, Simon %A Hind, Sarah %A Kraus, Christine %A Torre Diaz, Susana %A He, Bin %A Martin, Gregory %D 2016 %T MOESM3 of Detecting N-myristoylation and S-acylation of host and pathogen proteins in plants using click chemistry %U https://springernature.figshare.com/articles/journal_contribution/MOESM3_of_Detecting_N-myristoylation_and_S-acylation_of_host_and_pathogen_proteins_in_plants_using_click_chemistry/4338953 %R 10.6084/m9.figshare.c.3603188_D1.v1 %2 https://springernature.figshare.com/ndownloader/files/7062743 %K Fatty acylation %K Myristoylation %K Palmitoylation %K Stearylation %K S-acylation %K Click chemistry %K Plasma membrane %K Pathogen effectors %K Pattern recognition receptors %K Resistance proteins %K Arabidopsis thaliana %K Nicotiana benthamiana %X Additional file 3: Figure S3. Protein capture by means of myristoylation provides a potential method for the enrichment and investigation of the plant myristoylome. (A) Modified experimental scheme to capture and enrich myristoylated proteins using AvrPto as a test protein. (B) Nicotiana benthamiana was used to transiently express HA epitope-tagged avrPto. 50 μM Alk12 was infiltrated twice, 24 h after Agrobacterium infiltration and 6 h before sampling. Tissue was collected 48 h after transformation, total protein extracted, and a biotin tag added using click chemistry. Streptavidin affinity purification was used to enrich biotinylated proteins and AvrPto was detected using anti-HA western blotting. Input shows AvrPto levels before affinity purification. %I figshare