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. 2015 May 1;26(9):1764–1781. doi: 10.1091/mbc.E14-10-1475

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© 2015 Ghosh, de Campos, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 7: — Homo-oligomerization of class I nodulins. (A) Purified recombinant histidine (His)-tagged AtSfh1 (solubilized in 8 M urea) and soluble AtSfh3 nodulins (5 μg) were resolved by SDS–PAGE and visualized by Coomassie blue staining (left) and immunoblotting with anti-His tag antibody (middle). Right, immunoblotting of purified AtSfh1 nodulin with polyclonal AtSfh1 nodulin antibody (load at bottom). SDS-resistant homo-oligomeric forms are identified in all panels (asterisks). (B) Gel filtration chromatogram for purified native AtSfh3 nodulin. Top, immunoblot profile across the elution, shown above the chromatogram; elution properties of the indicated standards are identified by arrows. (C) Immunoblots of gel filtration column fractions of total lysates from yeast expressing myc-tagged AtSfh1 nodulin. Bottom, elution volume (milliliters); top, corresponding apparent molecular masses. Presumptive oligomeric states are identified at bottom. Brackets denote higher-order complexes. (D) Immunoblot profiles of gel filtration column fractions of lysates from tobacco leaf tissues expressing mRFP-tagged AtSfh1 WT, AtSfh1^K1-4A, and AtSfh1^K1-7A nodulins using anti-mRFP antibodies to visualize nodulin chimeras. Peak fractions of homo-oligomeric forms are identified (asterisks). Monomeric and presumed homo-oligomeric forms of the mRFP-tagged proteins are identified (arrows).