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. Author manuscript; available in PMC: 2018 Jan 20.
Published in final edited form as: ACS Synth Biol. 2016 Aug 9;6(1):39–44. doi: 10.1021/acssynbio.6b00160

Figure 3.

Figure 3

Experiments showing that GrsA and GrsB1 are present in their active (holo) forms. Panel A shows the fluorescent labeling of GrsA and GrsB1 on the thiolation domain active sites with a conjugated Bodipy-CoA fluorophore (see Figure S3 for complete gel image). Panel B top shows the MS2 spectrum resulting from the fragmentation of a precursor peptide containing the GrsA phosphopantetheine modification. Panel B bottom shows the MS2 spectrum for the corresponding GrsB1 T-domain peptide, indicating the mass of the observed pantetheine-derived ion.