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. 2012 Feb 22;7(2):e32305. doi: 10.1371/journal.pone.0032305

Figure 3. CsHMG shows identity to plant HMGBs of group B.

Figure 3

(A) Schematic representation of the CsHMG primary structure showing its central HMG-box domain flanked by the basic K-rich N-terminal and the acidic DE-rich C-terminal. (B) Phylogenetic analysis of plant HMGB proteins showing that CsHMG belongs to group B HMGBs. (C) Western-blot detection of the recombinant 6xHis-CsHMG (∼22 kDa) made in bacteria compared to bands detected in citrus cell extracts with the expected molecular size for the endogenous CsHMG (∼16 kDa). The anti-CsHMG serum also cross-reacted with a band of similar size in the cell extracts of A. thaliana wild-type and heterozygous hmg-b1 mutant. This band, which has the expected molecular weight for AtHMGB1 (∼18 kDa), is less pronounced in the heterozygous hmgb-1 mutant, thus indicating that CsHMG is structurally related to AtHMGB1.