Plasma membrane calcium ATPases are important components of ...

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Supplementary figure 2.AB
Figure S2. Identification of ACA8 and ACA10 peptides by mass-spectrometry analysis ofimmuno-purified FLS2-GFP. 21 in vitro grown seedlings were used either untreated or treated withflg22. Sample preparations, immuno-purifications and MS/MS analysis were performed essentiallyas described in Roux et al. (2011). Briefly, immuno-purifications of GFP-tagged proteins weredone using the magnetic GFP-trap system from Miltenyi Biotech using an IGEPAL-solubilisedprotein extract (4 mg protein per mL). Beads were washed with 0.1% IGEPAL extraction bufferprior to elution in boiling Laemli buffer. A. Peptide coverage of ACA8 and ACA10 proteinsidentified in an FLS2-GFP immuno-purified complex. Peptides found in untreated samples arehighlighted in green, peptides found in flg22-elicited samples are in orange, peptides found in bothconditions are indicated in blue, peptides found in all biological replicates of untreated and treatedsamples are shown in bold. B. Tryptic peptides identified by HPLC-electrospray ionization-MS/MS analysis. Peptides occurring in all biological replicates are marked in bold. Reproducibility( a ) of specific tryptic peptides out of three biological replicates of untreated or flg22-treatedsamples prepared from Arabidopsis plants expressing FLS2-GFP. In brackets, no peptides weredetected in technical controls using wild-type plants (n=2) or plants expressing a plasmamembrane addressed GFP (Lti6b-GFP; n=1).
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