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. Author manuscript; available in PMC: 2012 Sep 1.

Published in final edited form as: Mol Microbiol. 2011 Jul 28;81(5):1190–1204. doi: 10.1111/j.1365-2958.2011.07742.x

Immunoprecipitated subunits of RNAP were separated by SDS-PAGE. The α bands were excised and tryptically digested as described previously (Chi et al., 2010). The resulting peptides were analyzed in a LTQ OrbitrapXL™ mass spectrometer as described in the Materials and Methods. The double charged acetyllysine-modified peptides TPNLGK₂₉₇(+42)K and K₂₉₈(+42)SLTEIK were detected as mass peaks of m/z=400.237 and m/z=430.7582, respectively, in the digested α sample. A and D) The Xcorr and ΔCn scores, the actual peptide masses and mass deviations of the acetylated peptides. B and E) The corresponding CID MS/MS spectra. C and F) Complete b and y fragment ion series for these peptides.

Immunoprecipitated subunits of RNAP were separated by SDS-PAGE. The α bands were excised and tryptically digested as described previously (Chi et al., 2010). The resulting peptides were analyzed in a LTQ OrbitrapXL™ mass spectrometer as described in the Materials and Methods. The double charged acetyllysine-modified peptides TPNLGK₂₉₇(+42)K and K₂₉₈(+42)SLTEIK were detected as mass peaks of m/z=400.237 and m/z=430.7582, respectively, in the digested α sample. A and D) The Xcorr and ΔCn scores, the actual peptide masses and mass deviations of the acetylated peptides. B and E) The corresponding CID MS/MS spectra. C and F) Complete b and y fragment ion series for these peptides.