Figure 1.

Topology of proteolipid constructs and alignment of the VHA-c" and VHA-e amino acid sequences. (A) Transmembrane topology and localisation of conserved glutamate residues in various proteolipid isoforms or synthetic constructs, namely VHA-c3, VHA-c", VHA-ctrunc, VHA-c"trunc and hybrid proteolipid subunit. The functional Glu is highlighted in black, nonfunctional in grey. (B) VHA-c" sequences from S. cerevisiae (Vma16, Q91V37) and A. thaliana (VHA-c"1: At4g32530, CAB79970; VHA-c"2: At2g25610, NP_180132). (C) VHA-e sequences from S. cerevisiae (Vma9p, NP_958835), Bos taurus (M9.2, CAA75570), Manduca sexta (M9.7, CAA06822) and both VHA-e isoforms in A. thaliana (isoform 1: At5g55290, NP_568823; isoform 2: At4g26710, CAB79526) were compared. The sequences were obtained from the NCBI database and aligned using the ClustalW program. Transmembrane segments were predicted using HMMTOP and marked by bars. Identical amino acid residues are marked by (*) and highlighted in black, similar residues by (:).

Seidel et al. BMC Cell Biology 2008 9:28   doi:10.1186/1471-2121-9-28
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