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. Author manuscript; available in PMC: 2008 Aug 31.
Published in final edited form as: Cell Commun Adhes. 2008 May;15(1):85–93. doi: 10.1080/15419060802013588

Figure 1.

Figure 1

N-terminal sequences of human Cx26 genes studied in this work, and confocal and electron microscopy of Cx26M34Adel2-7 mutant. Sequence alignment of first 35 amino acid residues of two Cx26 N-termini, Cx26M34A and Cx26M34Adel2-7, is shown in (a). Both sequences contain the M34A point mutation. (b) Confocal micrograph of a transiently expressed Cx26M34Adel2-7-GFP in HeLa cells. Gap junction plaque formation between the adjacent cells was determined with the GFP fluorescence (arrows). The scale bar corresponds to 10 μm. Isolated membrane fractions (c), purified channels (d) and 2D crystal (e) of Cx26M34Adel2-7 were negatively stained with uranyl acetate and observed by conventional EM. This deletion mutant appears to form gap junction plaques. Cx26M34Adel2-7 channels are stable in detergent solution and appear as homogeneous doughnut-shaped particles. The orthorhombic crystal lattice of Cx26M34Adel2-7 is the same packing as Cx26M34A 2D crystals (Oshima et al., 2003). Scale bars for (c-e) represents 100 nm.