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. Author manuscript; available in PMC: 2013 Nov 1.
Published in final edited form as: Mol Microbiol. 2012 Oct 9;86(4):971–987. doi: 10.1111/mmi.12038

Figure 2.

Figure 2

HvJAMM1 is a Zn2+-dependent JAMM metalloprotease. Desampylation activity of HvJAMM1 was monitored using Flag-SAMP1 S85K (A) and Flag-SAMP2 (B) conjugates as described in Experimental Procedures. Similar results were observed for Flag-SAMP1 conjugates. EDTA was included as a negative control to disrupt HvJAMM1 activity based on the conservation of residues in the HvJAMM1 amino acid sequence that are likely to coordinate a catalytic zinc ion. Total protein was stained with Sypro Ruby to confirm equal loading and qualitatively assess whether or not HvJAMM1 is a non-specific protease that hydrolyzes the cellular proteome.