pgen.1006556.g003.tif (334.62 kB)
Mass spectrometry of 6His-SipB and endogenous SipB purified from S. Typhimurium.
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posted on 2017-01-13, 17:38 authored by Julie P. Viala, Valérie Prima, Rémy Puppo, Rym Agrebi, Mickaël J. Canestrari, Sabrina Lignon, Nicolas Chauvin, Stéphane Méresse, Tâm Mignot, Régine Lebrun, Emmanuelle BouveretMALDI-TOF mass spectrometry analysis of intact purified SipB. On the upper left of each graph is indicated the version of the purified SipB protein that has been analyzed by MALDI-TOF mass spectrometry and the organism from which it was purified: Stm for S. Typhimurium. A. The protein 6His-SipB was produced in the S. Typhimurium ΔiacP genetic background from production plasmids co-expressing iacP or not (S2B Fig for production plasmids); B. The intact native SipB was purified from S. Typhimurium WT and ΔiacP (strains JV1 and JV52) using an immunosorbent.
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Dedicated Acyl Carrier Proteintandem affinity purificationSPItranslocon protein SipBacylationtype 3 secretion systemsType 3 Secretion System Transloconacyl carrier proteinsIacPSalmonella pathogenicity island 1T 3SShost plasma membranemodificationT 3SS Cooccurrenceprotein lipidation pathwaysacyl carrier protein
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