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. Author manuscript; available in PMC: 2016 Feb 26.
Published in final edited form as: New Phytol. 2015 Jun 23;208(4):1157–1168. doi: 10.1111/nph.13528

Fig. 6.

Fig. 6

S349 and S351 affect the interaction of HopZ1a with inositol hexakisphosphate (IP6). (a) Analysis of the protein conformations of HopZ1a, HopZ1a(C216A) and HopZ1a(S349AS351A) in the presence or absence of IP6 by 1D 1H nuclear magnetic resonance (NMR). Protein spectra of the aromatic region in the presence (upper traces) or absence (lower traces) of IP6 are shown. Spectral changes specifically induced by IP6 in HopZ1a and HopZ1a(C216A) are indicated by arrows. (b) In vitro acetylation assays of HopZ1a, HopZ1a(C216A) and HopZ1a(S349AS351A) in the presence or absence of IP6. Numbers underneath the autoradiograph indicate relative acetylation levels of HopZ1a mutants compared with wild-type protein in the absence of IP6 (100%). Equal loading of the proteins was confirmed by Coomassie Blue staining. The experiment was repeated twice with similar results.